|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
54-343 |
1.05e-50 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 180.92 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
11-276 |
5.31e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.91 E-value: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 171 KKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNG 250
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
|
250 260
....*....|....*....|....*.
gi 1387230349 251 QDAVVNELTDYGANVNQPNNSGFTPL 276
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
22-307 |
8.19e-49 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 175.53 E-value: 8.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 182 YMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387230349 262 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
1-243 |
1.90e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.59 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 1 MAVLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHR 80
Cdd:COG0666 47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 81 AVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 161 AKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN 240
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
...
gi 1387230349 241 TAL 243
Cdd:COG0666 287 TLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
86-359 |
2.19e-38 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 150.18 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095 26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 236 NVYGNTALHLACYNGQD--AVVNELTDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1387230349 313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
22-310 |
2.36e-38 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 150.18 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 22 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 176 ALHwaAYMGH----LDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHLACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 250 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
153-507 |
5.26e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 144.33 E-value: 5.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrkll 392
Cdd:COG0666 150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 393 ssgfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGR 472
Cdd:COG0666 179 -----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
|
330 340 350
....*....|....*....|....*....|....*
gi 1387230349 473 TALHYAAASDMDRKSKIILGNAHENSEELERAREL 507
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
480-750 |
7.09e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 480 ASDMDRKSKIILGNAHENSEELERARELKEKEAALCLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSV 559
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 560 FEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPL 639
Cdd:COG0666 81 NAKDDGGNT--LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 640 HASVINGHTLCMRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE 718
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
|
250 260 270
....*....|....*....|....*....|..
gi 1387230349 719 CVQMLLEQEVSILCKDSRGRTPLHYAAARGHA 750
Cdd:COG0666 234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
55-301 |
1.58e-35 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 140.57 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100 16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLVNHGAEVTCKDKk 205
Cdd:PHA03100 96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHG 285
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
|
250
....*....|....*.
gi 1387230349 286 ALcLELLVNNGADVNI 301
Cdd:PHA03100 239 EI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
653-980 |
5.42e-34 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 132.39 E-value: 5.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 653 LLLEIADNPEVVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILC 732
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 733 KDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrtfignpftplhca 812
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 813 iindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDIL 892
Cdd:COG0666 143 -------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 893 VNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAV 972
Cdd:COG0666 206 LE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
|
....*...
gi 1387230349 973 DENGHTPA 980
Cdd:COG0666 282 LLDLLTLL 289
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
26-364 |
2.86e-33 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 137.89 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 26 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876 243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 185 H-LDVVALLVNHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 263 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
|
330 340
....*....|....*....|...
gi 1387230349 342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876 479 PLLIA--LEYHGIVNILLHYGAE 499
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
16-367 |
1.73e-32 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 132.01 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 16 IFSGDPEEIRMLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874 9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874 89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 175 RALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAV 254
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 255 VNELTDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1387230349 333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
352-670 |
3.28e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.38 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 352 ELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADF 431
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 432 HKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYAAasdmdrkskiilgnaHENSEELerarelkeke 511
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA---------------YNGNLEI---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 512 aalcLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEVLLQSL 591
Cdd:COG0666 136 ----VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGET--PLHLAAENGHLEIVKLLLEAG 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 592 VDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPLHASVINGHTLCMRLLLEIADNPEVVDVKDAK 670
Cdd:COG0666 210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
253-555 |
3.47e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 127.38 E-value: 3.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 253 AVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYAAASDMDRkskiilg 492
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE------- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 493 nahenseelerarelkekeaalCLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER 555
Cdd:COG0666 234 ----------------------IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
549-827 |
5.38e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.61 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 549 LELLLERTNSVFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIF 628
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 629 VKDNvTKRTPLHASVINGHTLCMRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTAL 708
Cdd:COG0666 82 AKDD-GGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 709 HRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENC 788
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE---AGADVNAKDNDGKTALDLAAENGNLEI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387230349 789 IEVLLEQKCFRTFIGNP-FTPLHCAIINDHENCASLLLGA 827
Cdd:COG0666 235 VKLLLEAGADLNAKDKDgLTALLLAAAAGAALIVKLLLLA 274
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
479-741 |
7.44e-32 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 126.22 E-value: 7.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 479 AASDMDRKSKIILGNAHENSEELERARELKEKEAALCLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNS 558
Cdd:COG0666 33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 559 VFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTP 638
Cdd:COG0666 113 VNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 639 LHASVINGHTLCMRLLLE-IADnpevVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHE 717
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
|
250 260
....*....|....*....|....
gi 1387230349 718 ECVQMLLEQEVSILCKDSRGRTPL 741
Cdd:COG0666 266 LIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
56-385 |
2.38e-31 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 131.72 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLVNHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHLACY--NGQDAVVNeLTDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
|
330
....*....|....*..
gi 1387230349 369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876 473 NIQNQYPL-LIALEYHG 488
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
689-998 |
4.25e-31 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 124.30 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 689 LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDcsf 768
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 769 KDNQGYTPLHWACYNGNENCIEVLLEQkcfrtfignpftplhcaiindhencaslllGAIdssiVNCRDDKGRTPLHAAA 848
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEA------------------------------GAD----VNARDKDGETPLHLAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 849 FADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILD 928
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 929 KIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 998
Cdd:COG0666 208 AGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
123-465 |
1.02e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 126.72 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCK 202
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ-DAVVNELTDYGANVNQPNNSGFTPLHFAAA 281
Cdd:PHA02876 241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 361 SGADtakcgihsmfplhLAALNahsdccrkllssgfeidtpDKFGrTCLHAAAAGGN-VECIKLLQSSGADFHKKDKCGR 439
Cdd:PHA02876 397 YGAD-------------IEALS-------------------QKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS 443
|
330 340
....*....|....*....|....*..
gi 1387230349 440 TPLHYAAA-NCHFHCIETLVTTGASVN 465
Cdd:PHA02876 444 TPLHYACKkNCKLDVIEMLLDNGADVN 470
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
212-475 |
7.85e-28 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.59 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095 20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387230349 440 TPLHYAAANCHFHCIETLVTTGASVNETDDWGRTAL 475
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
12-265 |
3.09e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 119.01 E-value: 3.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 167 NAFDKKDRRALHWAAY-MGHLDVVALLVNHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876 402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481
|
250 260
....*....|....*....|.
gi 1387230349 245 LACynGQDAVVNELTDYGANV 265
Cdd:PHA02876 482 IAL--EYHGIVNILLHYGAEL 500
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
192-465 |
1.28e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 113.99 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 192 LVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLAC---YNGQDAV--VNELTDYGANVN 266
Cdd:PHA03100 21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 267 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 346 aaryghelLINTLITSGAD-TAKCGIHSmfplhlaalnahsdccrkLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:PHA03100 158 --------ILKLLIDKGVDiNAKNRVNY------------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1387230349 425 QSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVN 465
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
75-346 |
5.71e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 113.05 E-value: 5.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLVNHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878 113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 226 LNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387230349 305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878 268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
28-238 |
2.35e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 110.14 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 28 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100 21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100 101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 172 ---------KDRR---ALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100 179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
355-665 |
6.73e-23 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 103.57 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095 30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 431 FHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGASVNETDDWGRTALHyaaasdmdrkskIILGNAHENSEelerarelk 508
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVE--------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 509 ekeaalCLEFLLQHDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEV 586
Cdd:PHA03095 169 ------LLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PLHSMATGSSCKRSLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 587 --LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCMRLLLEIADNPEVV 664
Cdd:PHA03095 241 lpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
.
gi 1387230349 665 D 665
Cdd:PHA03095 320 A 320
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
290-608 |
1.89e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.58 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 290 ELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTakcg 369
Cdd:PHA02874 19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 370 ihSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PHA02874 95 --SILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 450 HFHCIETLVTTGASVNETDDWGRTALHYAAasdmdrkskiilgnahenseelerarelkEKEAALCLEFLLQHDANPSIR 529
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAA-----------------------------EYGDYACIKLLIDHGNHIMNK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 530 DKEGYNSIHYAAAYgHRQCLELLLerTNSVFEESD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDL 607
Cdd:PHA02874 220 CKNGFTPLHNAIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDT 294
|
.
gi 1387230349 608 A 608
Cdd:PHA02874 295 A 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
22-295 |
7.33e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 100.34 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878 18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878 98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 229 GVEID-EINVYGNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878 258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
144-236 |
6.33e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.25 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 224 HLLNLGVEIDEIN 236
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
24-235 |
1.37e-20 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 96.25 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 24 IRMLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 176 ALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
177-269 |
2.83e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.32 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 177 LHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHLACYNGQDAVVN 256
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 257 ELTDYGANVNQPN 269
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
48-266 |
2.77e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 91.59 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKG 206
Cdd:PHA02875 89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHLACYNGQDAVVNELTDYGANVN 266
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
111-203 |
3.19e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 191 LLVNHGAEVTCKD 203
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
220-546 |
6.15e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 90.79 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 220 NVVKHLLN-LGVEIDEINvygnTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLhFAAASTHGALCLELLVNNGAD 298
Cdd:PHA02874 19 KIIKNKGNcINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 299 VNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL 378
Cdd:PHA02874 94 TSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 379 AALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAanCHFHCIETLV 458
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 459 TTGASVNETDDWGRTALHYAAASDMDRKskiilgnahenseelerarelkekeaalCLEFLLQHDANPSIRDKEGYNSIH 538
Cdd:PHA02874 242 INNASINDQDIDGSTPLHHAINPPCDID----------------------------IIDILLYHKADISIKDNKGENPID 293
|
....*...
gi 1387230349 539 YAAAYGHR 546
Cdd:PHA02874 294 TAFKYINK 301
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
618-981 |
8.87e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.66 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 618 EALINQGASIFVKDnVTKRTPLHASVINGHTLCMRLLLEIADNPEVVDVKDAkgqTPLMLAVAYGHSDAVSLLLEKEANV 697
Cdd:PHA02876 162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 698 DAVDImgctALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAargHATWLSELLQMALSE-EDCSFKDNQGYTP 776
Cdd:PHA02876 238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 777 LHWACYNGNencievlleqkcfrtfignpftplhcaiinDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFAD-HVEC 855
Cdd:PHA02876 311 LYLMAKNGY------------------------------DTENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 856 LQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGHEKCALLILdkIQDESL 935
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1387230349 936 INAKNNALQTPLHVAARNGLKV-VVEELLAKGACVLAVDENGHTPAL 981
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLL 481
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
572-880 |
1.84e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 89.25 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 572 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 649
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 650 CMRLLLEIADNPEVVDVKDAKgqtplmlavayghSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVS 729
Cdd:PHA02874 83 IIKLLIDNGVDTSILPIPCIE-------------KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 730 ILCKDSRGRTPLHYAAARGHATWLSELLQMALSeedCSFKDNQGYTPLHWACYNGNENCIEVLLEQ------KCfrtfiG 803
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY---ANVKDNNGESPLHNAAEYGDYACIKLLIDHgnhimnKC-----K 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 804 NPFTPLHCAIIndHENCASLLLgaIDSSIVNCRDDKGRTPLH-AAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMA 880
Cdd:PHA02874 222 NGFTPLHNAII--HNRSAIELL--INNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
389-665 |
1.89e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 89.34 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 389 RKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET---LVTTGAS 463
Cdd:PHA03100 19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEIvklLLEYGAN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 464 VNETDDWGRTALHYAAASDMdRKSKIIlgnahenseelerarelkekeaalclEFLLQHDANPSIRDKEGYNSIHYAAAY 543
Cdd:PHA03100 99 VNAPDNNGITPLLYAISKKS-NSYSIV--------------------------EYLLDNGANVNIKNSDGENLLHLYLES 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 544 GHR--QCLELLLERTNSVfeesdSGATKsplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 621
Cdd:PHA03100 152 NKIdlKILKLLIDKGVDI-----NAKNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL 212
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387230349 622 NQGASIFVKDNVTKrTPLHASVINGHTLCMRLLLEIADNPEVVD 665
Cdd:PHA03100 213 DLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
376-468 |
2.96e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.55 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 376 LHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIE 455
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 456 TLVTTGASVNETD 468
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
605-701 |
5.92e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 605 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCMRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHS 684
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1387230349 685 DAVSLLLEKEANVDAVD 701
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
652-999 |
7.80e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.77 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 652 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGHS---DAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 727
Cdd:PHA03095 32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 728 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCsfkDNQGYTPLHwaCYNGNENC-IEVLleqkcfrtfign 804
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnVELL------------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 805 pftplhcaiindhencaSLLLGAIdSSIVNcRDDKGRTPLH--AAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAE 882
Cdd:PHA03095 171 -----------------RLLIDAG-ADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 883 ngqagavdilvnsaqadltvkdkdlntslhlasskgHEKC-ALLILDKIQDESLINAKNNALQTPLHVAARNGLKVVVEE 961
Cdd:PHA03095 232 ------------------------------------GSSCkRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRR 275
|
330 340 350
....*....|....*....|....*....|....*...
gi 1387230349 962 LLAKGACVLAVDENGHTPALACAPNKDVaDCLALILAT 999
Cdd:PHA03095 276 LIALGADINAVSSDGNTPLSLMVRNNNG-RAVRAALAK 312
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
45-170 |
1.20e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1387230349 125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796 61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
389-726 |
3.40e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 85.85 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 389 RKLLSSGFEIDTPDKFGRTCLHAAAAGGNVEC---IKLLQSSGADFHKKDKCGRTPLH-YAAANCHFHCIETLVTTGASV 464
Cdd:PHA03095 31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 465 NETDDWGRTALHYAAASDmdrkskiilgNAHENseelerarelkekeaalCLEFLLQHDANPSIRDKEGYNSIHyaaayg 544
Cdd:PHA03095 111 NAKDKVGRTPLHVYLSGF----------NINPK-----------------VIRLLLRKGADVNALDLYGMTPLA------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 545 hrqcleLLLERTNSVFEesdsgatksplhlaaynghhqALEVLLQSLVDLDIRDEKGRTALD--LAAFKGHTECVEALIN 622
Cdd:PHA03095 158 ------VLLKSRNANVE---------------------LLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 623 QGASIFVKdNVTKRTPLHASVIngHTLCMRLLLE--IADNPEVvDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAV 700
Cdd:PHA03095 211 AGCDPAAT-DMLGNTPLHSMAT--GSSCKRSLVLplLIAGISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
|
330 340
....*....|....*....|....*.
gi 1387230349 701 DIMGCTALHRGIMTGHEECVQMLLEQ 726
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
182-697 |
4.00e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 86.66 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 182 YMGHLDVVALLVN-----HGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYG-NTALHLACY--NGQD 252
Cdd:PHA02876 12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 253 AVVNELTDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 325
Cdd:PHA02876 91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 326 IQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRK--------------- 390
Cdd:PHA02876 165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsl 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 391 --------------LLSSGFEIDTPDKFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 453
Cdd:PHA02876 245 lkairnedletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 454 IETLVTTGASVNETDDWGRTALHyaAASDMDRKSKIILGnahenseelerarelkekeaalclefLLQHDANPSIRDKEG 533
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT--------------------------LLELGANVNARDYCD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 534 YNSIHYAAAyghrqclellleRTNSVFeesdsgatksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALDLAAFKGH 613
Cdd:PHA02876 376 KTPIHYAAV------------RNNVVI-----------------------INTLLDYGADIEALSQKIGTALHFALCGTN 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 614 T-ECVEALINQGASIFVKdNVTKRTPLHASVINGHTL-CMRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYgHSdAVSLLL 691
Cdd:PHA02876 421 PyMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEY-HG-IVNILL 494
|
....*.
gi 1387230349 692 EKEANV 697
Cdd:PHA02876 495 HYGAEL 500
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
777-870 |
4.15e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.46 E-value: 4.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 777 LHWACYNGNENCIEVLLEQKC-FRTFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 855
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1387230349 856 LQLLLRHNAQVNAAD 870
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
572-665 |
8.36e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 76.31 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 572 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCM 651
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1387230349 652 RLLLEIADNPEVVD 665
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
587-890 |
9.02e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 84.31 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 587 LLQSLVDLDIRDEKGRTALDLAAFKGH---TECVEALINQGASIFVKDnVTKRTPLHASVINGHTL-CMRLLLEI-ADnp 661
Cdd:PHA03095 33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKAgAD-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 662 evVDVKDAKGQTPL--MLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALH-----RGIMTgheECVQMLLEQEVSILCKD 734
Cdd:PHA03095 110 --VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 735 SRGRTPLHYAA--ARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNencievlleqkCFRTFIGNpftplhca 812
Cdd:PHA03095 185 DRFRSLLHHHLqsFKPRARIVRELIR---AGCDPAATDMLGNTPLHSMATGSS-----------CKRSLVLP-------- 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 813 iindhencasLLLGAIDssiVNCRDDKGRTPLH-AAAFADHVECLQlLLRHNAQVNAADNSGKTPLMMAAENGQAGAVD 890
Cdd:PHA03095 243 ----------LLIAGIS---INARNRYGQTPLHyAAVFNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
495-911 |
1.43e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 84.73 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 495 HENSEELERARELKEKEAALCLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSVFEESDSGATKspLHL 574
Cdd:PHA02876 140 NESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSV--LEC 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 575 AAYNGHHQALEVLLqslvdlDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD-NVTKRTPLHASViNGHTLCmRL 653
Cdd:PHA02876 218 AVDSKNIDTIKAII------DNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHAS-QAPSLS-RL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 654 LLEIADNPEVVDVKDAKGQTPLMLAVAYGH-SDAVSLLLEKEANVDAVDIMGCTALHRG-IMTGHEECVQMLLEQEVSIL 731
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 732 CKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCSFKDNqgyTPLHWACYNGNencievlleqkcfrtfignPFTPLHc 811
Cdd:PHA02876 370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TALHFALCGTN-------------------PYMSVK- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 812 AIINDHENcaslllgaidssiVNCRDDKGRTPLHAAAFAD-HVECLQLLLRHNAQVNAADNSGKTPLMMAAenGQAGAVD 890
Cdd:PHA02876 427 TLIDRGAN-------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVN 491
|
410 420
....*....|....*....|...
gi 1387230349 891 ILVNSAQA--DLTVKDKDLNTSL 911
Cdd:PHA02876 492 ILLHYGAElrDSRVLHKSLNDNM 514
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
12-104 |
2.19e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.15 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 92 VLIKHSADVNARD 104
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
74-281 |
2.41e-16 |
|
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: 83.91 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLH 211
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 281
Cdd:cd22192 175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
233-491 |
3.57e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 82.62 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878 111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 384 HSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC-HFHCIETLVTTGA 462
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGV 259
|
250 260 270
....*....|....*....|....*....|
gi 1387230349 463 SVN-ETDDWGRTALHYAAASdmDRKSKIIL 491
Cdd:PHA02878 260 DVNaKSYILGLTALHSSIKS--ERKLKLLL 287
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
537-631 |
3.74e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 537 IHYAAAYGHRQCLELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 616
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1387230349 617 VEALINQGASIFVKD 631
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
254-465 |
4.49e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.96 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 254 VVNELTDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875 17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:PHA02875 96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1387230349 413 AAGGNVECIKLLQSSGA--DFHKKDKCgRTPLHYAAANCHFHCIETLVTTGASVN 465
Cdd:PHA02875 176 MAKGDIAICKMLLDSGAniDYFGKNGC-VAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
639-734 |
4.55e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 639 LHASVINGHTLCMRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHSDAVSLLLEKeANVDAVDiMGCTALHRGIMTGHEE 718
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADA---NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 1387230349 719 CVQMLLEQEVSILCKD 734
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
20-170 |
5.04e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 82.24 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 20 DPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878 226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
17-168 |
1.16e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.84 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 17 FSGDPEEIRMLIHKTEDVNALDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
|
.
gi 1387230349 168 A 168
Cdd:PHA03095 285 A 285
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
708-797 |
1.28e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 708 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEdcsfkDNQGYTPLHWACYNGNEN 787
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75
|
90
....*....|
gi 1387230349 788 CIEVLLEQKC 797
Cdd:pfam12796 76 IVKLLLEKGA 85
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
844-940 |
1.29e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 844 LHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAQADLTVKDKdlnTSLHLASSKGHEKCA 923
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
|
90
....*....|....*..
gi 1387230349 924 LLILDKIQDeslINAKN 940
Cdd:pfam12796 78 KLLLEKGAD---INVKD 91
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
78-364 |
6.67e-15 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 78.72 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798 44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798 94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 232 IDEI-NVYGNTALHlaCY-----NGQDA-VVNELTDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798 174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798 244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
516-726 |
7.12e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 7.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 516 LEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSVFEESDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 593
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 594 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCMRLLLeiaDNPEVVDVKDAKGQT 673
Cdd:PHA02875 96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 674 PLMLAVAYGHSDAVSLLLEKEANVDAVDIMGC-TALHRGIMTGHEECVQMLLEQ 726
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
409-530 |
1.21e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 409 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgASVNETDDwGRTALHYAAASdmdrksk 488
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARS------- 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1387230349 489 iilgnaheNSEElerarelkekeaalCLEFLLQHDANPSIRD 530
Cdd:pfam12796 72 --------GHLE--------------IVKLLLEKGADINVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
550-710 |
1.63e-14 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 78.37 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 550 ELLLERTnsvfEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 629
Cdd:PLN03192 511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 630 KDnVTKRTPLHASVINGHTLCMRLLLEIA--DNPEV--------------------------VDVKDAKGQTPLMLAVAY 681
Cdd:PLN03192 587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHAagdllctaakrndltamkellkqglnVDSEDHQGATALQVAMAE 665
|
170 180 190
....*....|....*....|....*....|..
gi 1387230349 682 GHSDAVSLLLEKEANVDAV---DIMGCTALHR 710
Cdd:PLN03192 666 DHVDMVRLLIMNGADVDKAntdDDFSPTELRE 697
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
422-744 |
2.02e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 77.80 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 422 KLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYAAAS-DMDRKSKIILGNAHENSEE 500
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSkNIDTIKAIIDNRSNINKND 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 501 LERARELKEKEAALClefLLQHDANPSIRDKEGYNSihyaaayghrqclelllertnsvfeesdsgatkSPLHLAAYNGH 580
Cdd:PHA02876 242 LSLLKAIRNEDLETS---LLLYDAGFSVNSIDDCKN---------------------------------TPLHHASQAPS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 581 HQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGASIFVKDNVTKrTPLH-ASVINGHTLCMRLLLEI 657
Cdd:PHA02876 286 LSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI-TPLHqASTLDRNKDIVITLLEL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 658 ADNpevVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIM-TGHEECVQMLLEQEVSILCKDSR 736
Cdd:PHA02876 365 GAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKD 441
|
....*...
gi 1387230349 737 GRTPLHYA 744
Cdd:PHA02876 442 LSTPLHYA 449
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
675-749 |
2.07e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 2.07e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387230349 675 LMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 749
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
9-167 |
2.11e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 76.57 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 9 QPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228
|
.
gi 1387230349 167 N 167
Cdd:PHA02875 229 N 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
343-435 |
5.70e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgFEIDTPDKfGRTCLHAAAAGGNVECIK 422
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 423 LLQSSGADFHKKD 435
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
741-825 |
9.93e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 67.83 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 741 LHYAAARGHATWLSELLQmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRtFIGNPFTPLHCAIINDHENC 820
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGRTALHYAARSGHLEI 76
|
....*
gi 1387230349 821 ASLLL 825
Cdd:pfam12796 77 VKLLL 81
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
821-979 |
1.06e-13 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 73.06 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 821 ASLLLGAIDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAQADL 900
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 901 TVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTP 979
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
639-909 |
1.29e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 74.32 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 639 LHASVINGHTLCMRLLLE--IADNPEVVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH 716
Cdd:PHA03100 1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 717 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQMALseeDCSFKDNQGYTPLHWA--CYNGNEN 787
Cdd:PHA03100 81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 788 CIEVLLEqkcfrtfignpftplHCAIINDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVN 867
Cdd:PHA03100 158 ILKLLID---------------KGVDINAKNRVNYLLSYGVP---INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387230349 868 AADNSGKTPLMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 909
Cdd:PHA03100 220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
775-993 |
3.56e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 73.07 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 775 TPLHWACYNGNENCIEVLLEQKCFRTFIG-NPFTPLHCAI-INDHENCASLLLGAIDSSI-------------------- 832
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 833 VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLH 912
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 913 LASSKGHEKCALLILDkiqDESLINAKNNALQTPLHVAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 989
Cdd:PHA02874 196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 1387230349 990 ADCL 993
Cdd:PHA02874 271 IDIL 274
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
55-273 |
4.18e-13 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 72.95 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLVNHG 196
Cdd:PHA02798 132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798 210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387230349 238 YGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGF 273
Cdd:PHA02798 290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
515-598 |
1.10e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 515 CLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSvfEESDSGATksPLHLAAYNGHHQALEVLLQSLVDL 594
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLLEKGADI 87
|
....
gi 1387230349 595 DIRD 598
Cdd:pfam12796 88 NVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
48-201 |
1.29e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTC 201
Cdd:PLN03192 612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
877-973 |
6.43e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.44 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 877 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQdeslINAKNNAlQTPLHVAARNGLK 956
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
|
90
....*....|....*..
gi 1387230349 957 VVVEELLAKGACVLAVD 973
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
166-445 |
6.75e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.14 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 166 INAFDKKDRRA----------LHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878 20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 236 NVYgnTALHLACYNGQDAVVNE-LTDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 313
Cdd:PHA02878 100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 314 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHS-DCCRKLL 392
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLL 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 393 SSGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:PHA02878 256 EHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
140-193 |
1.14e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 1.14e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLV 193
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
310-402 |
1.21e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 61.67 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1387230349 390 KLLSSGFEIDTPD 402
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
174-226 |
1.34e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.34e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 174 RRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
527-704 |
1.93e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 67.30 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 527 SIRDKEGYNSIHYAAAYGHRQCLELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALD 606
Cdd:PHA02874 118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY--PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 607 LAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGhtlcmRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHS-D 685
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN-----RSAIELLINNASINDQDIDGSTPLHHAINPPCDiD 269
|
170
....*....|....*....
gi 1387230349 686 AVSLLLEKEANVDAVDIMG 704
Cdd:PHA02874 270 IIDILLYHKADISIKDNKG 288
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
405-458 |
1.98e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.98 E-value: 1.98e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 458
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
150-275 |
4.64e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 63.30 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLVNHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859 63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 224 HLLNLGVEIDEINVYGNTALH-LACYNGQDAVVNELTDYGANVNQPNNSGFTP 275
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
409-679 |
5.18e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.44 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 409 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVT--TGASVNETDDWGRTALHYAAASdmdrK 486
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsiNKCSVFYTLVAIKDAFNNRNVE----I 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 487 SKIILGNAHENSEELErARELKEKEAALCLE-----FLLQHDANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERTNSVf 560
Cdd:PHA02878 117 FKIILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSYGANV- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 561 eESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPL 639
Cdd:PHA02878 195 -NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTAL 273
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387230349 640 HASVINGHTLcmRLLLEIADNPEVVdvkDAKGQTPLMLAV 679
Cdd:PHA02878 274 HSSIKSERKL--KLLLEYGADINSL---NSYKLTPLSSAV 308
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
693-979 |
5.74e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.06 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 693 KEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALseedcsfKDNQ 772
Cdd:PHA02878 26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 773 GYT--PLHWACYNGNENCIEVLLEQKcfrtFIGNpftplhcAIINDHENCASLLLGAIDSSI----------VNCRD-DK 839
Cdd:PHA02878 99 FYTlvAIKDAFNNRNVEIFKIILTNR----YKNI-------QTIDLVYIDKKSKDDIIEAEItklllsygadINMKDrHK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 840 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGH 919
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 920 EKCALLILdkIQDESLINAKNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAVDENGHTP 979
Cdd:PHA02878 247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
243-336 |
8.60e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 59.36 E-value: 8.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 243 LHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 322
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1387230349 323 QTLIQNGGEIDCVD 336
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
764-975 |
1.33e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 764 EDCSFKDNqgYTPLHWACYNGNENCIEVLLEQKCF-RTFIGNPFTPLH-----CAIINDHENCASLLL--GAIdssiVNC 835
Cdd:PHA03100 28 NDYSYKKP--VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGAN----VNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 836 RDDKGRTPLHAAAFA--DHVECLQLLLRHNAQVNAADNSGKTPLMMAAENG------------------QAGAVDILVNS 895
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 896 AqADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDEN 975
Cdd:PHA03100 182 G-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
833-986 |
1.38e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 64.69 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 833 VNCRDDKGRTPLHAAAFADHV-----ECLQLLLRHNAQVNAADNSGKTPLMMAAEN--GQAGAVDILVNSAqADLTVKDK 905
Cdd:PHA03100 61 INSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 906 DLNTSLHLASSKGHEK---CALLILDK------------IQDESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 970
Cdd:PHA03100 140 DGENLLHLYLESNKIDlkiLKLLIDKGvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
|
170
....*....|....*..
gi 1387230349 971 AVDENGHTPA-LACAPN 986
Cdd:PHA03100 220 LVNKYGDTPLhIAILNN 236
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
665-793 |
1.40e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 65.66 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 665 DVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLleQEVSILCKDSRGRTPLHYA 744
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL--YHFASISDPHAAGDLLCTA 629
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1387230349 745 AARGHATWLSELLQMALseeDCSFKDNQGYTPLHWACYNGNENCIEVLL 793
Cdd:PLN03192 630 AKRNDLTAMKELLKQGL---NVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
153-315 |
1.69e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 64.24 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVT-CKDKKGYTPLHAAASNGQINVVKHLLNLGVE 231
Cdd:PHA02875 48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 232 IDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALClELLVNNGADVNIQSKDGKSPLH 311
Cdd:PHA02875 128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC-KMLLDSGANIDYFGKNGCVAAL 206
|
....
gi 1387230349 312 MTAV 315
Cdd:PHA02875 207 CYAI 210
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
744-910 |
2.10e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.89 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 744 AAARGHATWLSELLQMALseeDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRTFIGNpfTPLHCAIINDHENC 820
Cdd:PLN03192 532 VASTGNAALLEELLKAKL---DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 821 ASLLLGAIDSSIVNCRDDKgrtpLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILV-NSAQAD 899
Cdd:PLN03192 607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682
|
170
....*....|.
gi 1387230349 900 LTVKDKDLNTS 910
Cdd:PLN03192 683 KANTDDDFSPT 693
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
49-280 |
3.46e-10 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 64.33 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870 20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870 96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 177 ---LHWAAYMGHLDVVALLVNHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHLACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233
|
250 260 270
....*....|....*....|....*....|....
gi 1387230349 254 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
3-114 |
5.17e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 62.98 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275
|
90 100 110
....*....|....*....|....*....|....
gi 1387230349 81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878 276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
183-374 |
9.47e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 183 MGHLDVVALLVNHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 263 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
|
170 180 190
....*....|....*....|....*....|..
gi 1387230349 343 LHVAARYGHELLINTLITSGADTAKCGIHSMF 374
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
375-424 |
9.62e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 9.62e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 375 PLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
539-758 |
1.28e-09 |
|
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: 62.34 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 539 YAAAYGHRQCLELLL--ERTNsVFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 611
Cdd:cd22192 23 LAAKENDVQAIKKLLkcPSCD-LFQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 612 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCMRllleiadnpevvdvkdakGQTPLMLAVAYGHSDAVSLLL 691
Cdd:cd22192 100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387230349 692 EKEANVDAVDIMGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 758
Cdd:cd22192 157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
570-621 |
1.70e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 1.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 570 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 621
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
279-430 |
2.15e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.81 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 279 AAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTL 358
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 359 --ITSGADTAKCGIhsmfPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:PLN03192 611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
144-226 |
2.19e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.45 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
...
gi 1387230349 224 HLL 226
Cdd:PTZ00322 166 LLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
673-724 |
2.21e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.20 E-value: 2.21e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 673 TPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 724
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
147-305 |
2.80e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 61.42 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQ---INVVK 223
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHhkiFRILY 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 224 HLLNLGveideiNVY-GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQ 302
Cdd:PLN03192 612 HFASIS------DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKA 684
|
...
gi 1387230349 303 SKD 305
Cdd:PLN03192 685 NTD 687
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
107-359 |
2.97e-09 |
|
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: 60.80 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 107 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHVEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192 17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 183 mghlDVVALLVNHgaEVTCkdkkgytplhaaasngqinvvkhllnlgveideiNVY-GNTALHLACYNGQDAVVNELTDY 261
Cdd:cd22192 72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 262 GANVNQPNNSG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 326
Cdd:cd22192 112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387230349 327 --------QNGGEIDCV-DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192 191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
342-611 |
3.20e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.66 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 342 PLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLA-----------------------ALNAHSDCC--------RK 390
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemirsinkcsvfyTLVAIKDAFnnrnveifKI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 391 LLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDK-CGRTPLHYAAANCHFHCIETLVTTGASVNETDD 469
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 470 WGRTALHYAAasdmdrkskiilgnAHENSEelerarelkekeaalCLEFLLQHDANPSIRDKEGYNSIHYAAAY-GHRQC 548
Cdd:PHA02878 200 TNNSPLHHAV--------------KHYNKP---------------IVHILLENGASTDARDKCGNTPLHISVGYcKDYDI 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 549 LELLLERTNSVFEESdSGATKSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDLAAFK 611
Cdd:PHA02878 251 LKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
20-164 |
5.70e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 59.65 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
55-317 |
6.86e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 59.75 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 55 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 128
Cdd:PHA02989 51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 129 LLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKKDRRA---LH--WAAYMGHLDVVALLVNHGAEV-TCK 202
Cdd:PHA02989 115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 203 DKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL------HLACYNGQDAVVNELTDYgANVNQPNNSG 272
Cdd:PHA02989 178 SLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKG 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1387230349 273 FTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG 317
Cdd:PHA02989 257 FNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
823-899 |
8.48e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.53 E-value: 8.48e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387230349 823 LLLGAIDSsivNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAQAD 899
Cdd:PTZ00322 101 LLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
673-979 |
1.21e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 58.44 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 673 TPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 750
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 751 TWLSellqmalSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrtfignpftplhcaiindhencaslllgaids 830
Cdd:PHA02874 109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 831 SIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTS 910
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 911 LHLASSKGHEKCALLIldkiqDESLINAKNNALQTPLHVAARNGLKV-VVEELLAKGACVLAVDENGHTP 979
Cdd:PHA02874 227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENP 291
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
289-475 |
1.41e-08 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 59.16 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 364 DTAKCGIHSMFPLHLA-ALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV--ECIKLLQSSGADFHKKDKCGRT 440
Cdd:PHA02716 275 GNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNT 354
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387230349 441 PLH-YAAANCHFH-------------CIETLVTTGASVNETDDWGRTAL 475
Cdd:PHA02716 355 VLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
340-476 |
1.71e-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: 58.49 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDKF-GRTCLHAAA 413
Cdd:cd22192 18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387230349 414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALH 476
Cdd:cd22192 98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
53-312 |
1.92e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 58.14 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallvnhgaevTCKDKKGYTPLHA 212
Cdd:PHA02946 121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946 148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226
|
250 260
....*....|....*....|..
gi 1387230349 291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946 227 NLLLPSTDVNKQNKFGDSPLTL 248
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
636-748 |
2.00e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 57.69 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 636 RTPLHASVINGHTLCMRLLLEIadNPEVVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTG 715
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
|
90 100 110
....*....|....*....|....*....|...
gi 1387230349 716 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 748
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
323-554 |
2.08e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 57.76 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 323 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLH------------------------- 377
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtddevierinllvqygakinn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 378 ----------LAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:PHA02946 136 svdeegcgplLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLHIV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 446 AANCHFHC-IETLVTTGASVNETDDWGRTALHYAAASdmdrkskiiLGNAHENSEELERARELKEKEAALCLeFLLQHDA 524
Cdd:PHA02946 216 CSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT---------LSPAHLINKLLSTSNVITDQTVNICI-FYDRDDV 285
|
250 260 270
....*....|....*....|....*....|...
gi 1387230349 525 NPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 554
Cdd:PHA02946 286 LEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
11-147 |
2.11e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 57.67 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 90 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 147
Cdd:PHA02874 238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
274-443 |
2.13e-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: 58.10 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192 19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 348 RYGHELLINTLITSGADTAK---CGihSMFplhlaALNAHSDCcrkllssgfeidtpdKFGRTCLHAAAAGGNVECIKLL 424
Cdd:cd22192 98 VNQNLNLVRELIARGADVVSpraTG--TFF-----RPGPKNLI---------------YYGEHPLSFAACVGNEEIVRLL 155
|
170
....*....|....*....
gi 1387230349 425 QSSGADFHKKDKCGRTPLH 443
Cdd:cd22192 156 IEHGADIRAQDSLGNTVLH 174
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
603-785 |
2.88e-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: 57.72 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 603 TALDLAAFKGHTECVEALI-NQGASIFVKDNVTKrTPLHASVINGHTLCMRLLLEIAdnPEVVDVKDA----KGQTPLML 677
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 678 AVAYGHSDAVSLLLEKEANVDAVDIMGcTALHRGI---------------MTGHEECVQMLLEQEVSILCKDSRGRTPLH 742
Cdd:cd22192 96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 743 YAAARGHATWLSEL--LQMALSEEDCS-----FKDNQGYTPLHWACYNGN 785
Cdd:cd22192 175 ILVLQPNKTFACQMydLILSYDKEDDLqpldlVPNNQGLTPFKLAAKEGN 224
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
570-740 |
3.35e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.92 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 570 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 647
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 648 TLCMRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQE 727
Cdd:PHA02875 115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
170
....*....|...
gi 1387230349 728 VSIlckDSRGRTP 740
Cdd:PHA02875 192 ANI---DYFGKNG 201
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
109-160 |
3.60e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.74 E-value: 3.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
74-127 |
4.34e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
438-480 |
4.65e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 4.65e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1387230349 438 GRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYAAA 480
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
812-996 |
5.41e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.54 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 812 AIINDHENCASLLLgaiDSSI-VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVD 890
Cdd:PHA02875 9 AILFGELDIARRLL---DIGInPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 891 ILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVEELLAKGACVL 970
Cdd:PHA02875 86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLD 162
|
170 180
....*....|....*....|....*.
gi 1387230349 971 AVDENGHTPALACAPNKDVADCLALI 996
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLL 188
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
636-893 |
5.95e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 56.15 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 636 RTPLHASVINGHTLCMRLLLEIADNP--EVVDvkdakGQTPLMLAVAYGHSDAVSLLLEKEA--NVDAVDImgctalhrg 711
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 712 imtgheecvqmlleqevsilckdsrgRTPLHYAAARGHATWLSELLQMALSEEDCSFKDnqGYTPLHWACYNGNENCIEV 791
Cdd:PHA02875 69 --------------------------ESELHDAVEEGDVKAVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 792 LLEQKCfRTFIGNP--FTPLHCAIINDHENCASLLLGaiDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAA 869
Cdd:PHA02875 121 LIARGA-DPDIPNTdkFSPLHLAVMMGDIKGIELLID--HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYF 197
|
250 260
....*....|....*....|....*
gi 1387230349 870 DNSGKTPLM-MAAENGQAGAVDILV 893
Cdd:PHA02875 198 GKNGCVAALcYAIENNKIDIVRLFI 222
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
108-282 |
6.48e-08 |
|
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: 56.81 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882 27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 169 FDKKDRR--------ALHWAAYMGHLDVVALLVNHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882 107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 238 YGNTALHLACYNGqdavvneLTDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd21882 170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
12-97 |
8.03e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.45 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322 86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*.
gi 1387230349 92 VLIKHS 97
Cdd:PTZ00322 166 LLSRHS 171
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
323-687 |
8.19e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 56.13 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 323 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGfeIDTp 401
Cdd:PHA02874 18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDT- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 402 DKFGRTCLhaaaaggNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNetddwgrtalhyaaas 481
Cdd:PHA02874 95 SILPIPCI-------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN---------------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 482 dmdrkskiilgnahenseelerarelkekeaalclefllqhdanpsIRDKEGYNSIHYAAAYGHRQCLELLLErtNSVFE 561
Cdd:PHA02874 152 ----------------------------------------------IEDDNGCYPIHIAIKHNFFDIIKLLLE--KGAYA 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 562 ESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTeCVEALINQgASIFVKDnVTKRTPLHa 641
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINN-ASINDQD-IDGSTPLH- 259
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 642 svingHTLCMRLLLEIAD----NPEVVDVKDAKGQTPLMLAVAYGHSDAV 687
Cdd:PHA02874 260 -----HAINPPCDIDIIDillyHKADISIKDNKGENPIDTAFKYINKDPV 304
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
208-419 |
8.27e-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: 56.17 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGAN-VNQPNNS----GFTPLHFAAA 281
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVaa 347
Cdd:cd22192 99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 348 ryghellintLITSGADTAKCgihSMFPLHLaALNAHSDccrkllssGFEIDT-PDKFGRTCLHAAAAGGNVE 419
Cdd:cd22192 176 ----------LVLQPNKTFAC---QMYDLIL-SYDKEDD--------LQPLDLvPNNQGLTPFKLAAKEGNIV 226
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
77-250 |
9.80e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 53.67 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLVNHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859 101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
|
170 180
....*....|....*....|....*
gi 1387230349 226 LNLGVEIDEINVYGNTALHLACYNG 250
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDLIKFRN 203
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
549-796 |
1.08e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.66 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 549 LELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASI 627
Cdd:PHA02878 53 VKSLLTRGHNVNQPDHRDLT--PLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 628 FVKDNVTKRTPLHASVINghTLCMRLLLEIADNPEVVDvkDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTA 707
Cdd:PHA02878 129 QTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 708 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATwlsELLQMALSEEDCSFKDN--QGYTPLHWACYngN 785
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--S 279
|
250
....*....|.
gi 1387230349 786 ENCIEVLLEQK 796
Cdd:PHA02878 280 ERKLKLLLEYG 290
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
45-326 |
1.17e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 56.07 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 45 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 118
Cdd:PHA02716 181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 119 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 159
Cdd:PHA02716 259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 160 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLVNHGAEVTCKDKKGYTPLHAAASNGQ----- 218
Cdd:PHA02716 339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 219 -----------INVVKH--LLNLGVEIDE--------INVYG-NTALHLACYNGQDAVVNELTDYGANVNQPNN-----S 271
Cdd:PHA02716 417 diidclisdkvLNMVKHriLQDLLIRVDDtpciihhiIAKYNiPTDLYTDEYEPYDSTKIHDVYHCAIIERYNNavcetS 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 272 GFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716 497 GMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
7-114 |
1.30e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 55.27 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246
|
90 100 110
....*....|....*....|....*....|
gi 1387230349 86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
191-246 |
1.34e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 49.27 E-value: 1.34e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 191 LLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLA 246
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
840-893 |
1.43e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 1.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 840 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILV 893
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
11-171 |
1.61e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 52.90 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 11 PLVQAIFSGDPEEIRMLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859 99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176
|
170
....*....|....
gi 1387230349 158 LLLAKGANINAFDK 171
Cdd:PHA02859 177 FLTSLGIDINETNK 190
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
775-965 |
1.61e-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: 55.40 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 775 TPLHWACYNGNENCIEVLLeqKCFRTfigNPF-------TPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTP 843
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLL--KCPSC---DLFqrgalgeTALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 844 LHAAAFADHVECLQLLLRHNAQVNAADNSG--------------KTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNT 909
Cdd:cd22192 93 LHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyygEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 910 SLHLASSKGHEKCA------LLILDKIQDE-SLINAKNNALQTPLHVAARNGLKVVVEELLAK 965
Cdd:cd22192 172 VLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
411-627 |
1.71e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 411 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIetLVttgasvnetddwgrtalhyaaasdmdrkskii 490
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCV--LV-------------------------------- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 491 lgnahenseelerarelkekeaalclefLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSvfeeSDSGATKS 570
Cdd:PLN03192 577 ----------------------------LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI----SDPHAAGD 624
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387230349 571 PLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 627
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
706-749 |
1.91e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 1.91e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1387230349 706 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 749
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
281-350 |
2.00e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 2.00e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
206-251 |
2.39e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 2.39e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1387230349 206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ 251
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
42-94 |
3.71e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.65 E-value: 3.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
856-996 |
4.05e-07 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 53.03 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 856 LQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDesl 935
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD--- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 936 INAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALI 996
Cdd:COG0666 80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
69-198 |
4.40e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322 56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAE 198
Cdd:PTZ00322 124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
721-964 |
5.99e-07 |
|
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: 53.55 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 721 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 796
Cdd:TIGR00870 35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 797 CFRTFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 850
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 851 DHVECLQLLLRHNAQVNAADNSGKTPLMMAAEngqagavdilvnsaQADLTVKDKDLNTSLHLAsskghekcALLILDKI 930
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKL 243
|
250 260 270
....*....|....*....|....*....|....*
gi 1387230349 931 QD-ESLINAKNNALQTPLHVAARNGLKVVVEELLA 964
Cdd:TIGR00870 244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
338-480 |
6.19e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.07 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 338 DGNTPLHVAARYGHELLINTLITSGA--DTAKCGIHSmfPLHLAALNAHSDCCRKLLSSG-FEIDTPDKFGRTCLHAAAA 414
Cdd:PHA02875 34 DGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGkFADDVFYKDGMTPLHLATI 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 415 GGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYAAA 480
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMA 177
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
377-499 |
7.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 377 HLAALNAHSDccrKLLSSGFEIDTPDKFGRTCLHAA-------AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PTZ00322 50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 450 HFHCIETLVTTGASVNETDDWGRTALHYAAASDMDRKSKIILGNAHENSE 499
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-160 |
9.57e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 22 EEIRMLIHKTEDVNALDSEKRTPLHVAAflgDAEIIELLILsgarvnakdNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:PTZ00322 42 EEIARIDTHLEALEATENKDATPDHNLT---TEEVIDPVVA---------HMLTVELCQLAASGDAVGARILLTGGADPN 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
807-860 |
9.80e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.50 E-value: 9.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 807 TPLHCAIINDHENCASLLLGAidSSIVNCRDDKGRTPLHAAAFADHVECLQLLL 860
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-261 |
1.21e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 1.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 189 VALLVNHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
570-814 |
1.40e-06 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 52.39 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 570 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 636
Cdd:TIGR00870 54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 637 TPLHASVINGHTLCMRLLLEIADNPEV----VDVKDAKGQT-------PLMLAVAYGHSDAVSLLLEKEANVDAVDIMGC 705
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 706 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQMALSEEDCSFKDNQGYTPLHWACYNGN 785
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269
|
250 260 270
....*....|....*....|....*....|
gi 1387230349 786 ENCIEVLLEQKCF-RTFIGNPFTPLHCAII 814
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
837-973 |
1.52e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 837 DDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAQADLTVKDKDLntsLHLASS 916
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAK 631
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 917 KGHekcaLLILDKIQDESL-INAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVD 973
Cdd:PLN03192 632 RND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
209-368 |
1.98e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.82 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHlACYNGQDAVVNE---LTDYGANVN-QPNNSGFTPLHFAAASTH 284
Cdd:PHA02859 24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859 100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179
|
....*....
gi 1387230349 360 TSGADTAKC 368
Cdd:PHA02859 180 SLGIDINET 188
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
10-61 |
2.35e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.73 E-value: 2.35e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
737-793 |
3.41e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 3.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 737 GRTPLHYAAARGHatwlSELLQMAL-SEEDCSFKDNQGYTPLHWACYNGNENCIEVLL 793
Cdd:pfam13637 1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
239-293 |
3.61e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 3.61e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1387230349 239 GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
140-168 |
4.02e-06 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 44.12 E-value: 4.02e-06
10 20
....*....|....*....|....*....
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
751-946 |
4.23e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 49.66 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 751 TWLSELLQMALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRTFIGNPFtPLH-CAIINDHENCASLLLGAID 829
Cdd:PHA02791 8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 830 SSIVncrDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSG-KTPLMMAAENGQAGAVDILVNSAQA--DLTVkdkd 906
Cdd:PHA02791 87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387230349 907 LNTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTP 946
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
308-359 |
4.23e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 4.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
533-588 |
5.96e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.57 E-value: 5.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 533 GYNSIHYAAAYGHRQCLELLLERTNSVFEESDSGATksPLHLAAYNGHHQALEVLL 588
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
20-295 |
6.42e-06 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 50.05 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946 51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946 131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 175 RALH--WAAYMGHLDVVALLVNhGAEVTCKDKKGYTPLHAAASNGQinvVKHLLNLGVEIDeiNVYGNTALHLACYNGQD 252
Cdd:PHA02946 210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLS---PAHLINKLLSTS--NVITDQTVNICIFYDRD 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387230349 253 AVVNELTDYGANVNQPNnsgftplhFAAASTHGAL-CLELLVNN 295
Cdd:PHA02946 284 DVLEIINDKGKQYDSTD--------FKMAVEVGSIrCVKYLLDN 319
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
544-783 |
7.25e-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: 49.88 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 544 GHRQCLELLLerTNSVFEESDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 609
Cdd:cd21882 6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 610 FKGHTECVEALINQGASIFVKDNVT--KRTPlhasvingHTLCMRllleiadnpevvdvkdakGQTPLMLAVAYGHSDAV 687
Cdd:cd21882 82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 688 SLLLE---KEANVDAVDIMGCTALHRGIMTGHEE------CVQM--LLEQEVSILC--------KDSRGRTPLHYAAARG 748
Cdd:cd21882 136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynLLLSYGAHLDptqqleeiPNHQGLTPLKLAAVEG 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 1387230349 749 HATWLSELLQMALSE--EDCSFKDNQ-GYTPLHWACYN 783
Cdd:cd21882 216 KIVMFQHILQREFSGpyQPLSRKFTEwTYGPVTSSLYD 253
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
158-213 |
8.25e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.26 E-value: 8.25e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-171 |
9.17e-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: 43.43 E-value: 9.17e-06
10 20 30
....*....|....*....|....*....|...
gi 1387230349 140 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 171
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
833-997 |
9.38e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 49.19 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 833 VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNS----------------- 895
Cdd:PHA02874 28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvdtsilpipciekdmi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 896 -----AQADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 970
Cdd:PHA02874 108 ktildCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
|
170 180
....*....|....*....|....*..
gi 1387230349 971 AVDENGHTPALACAPNKDVAdCLALIL 997
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYA-CIKLLI 210
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
881-976 |
1.13e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.51 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 881 AENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGHEKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVE 960
Cdd:PTZ00322 90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165
|
90
....*....|....*.
gi 1387230349 961 ELLAKGACVLAVDENG 976
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
140-282 |
1.63e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 49.03 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLVNHGAEVTC---- 201
Cdd:cd22196 47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALHL---ACYNGQD------AVVNELT 259
Cdd:cd22196 127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHAlveVADNTPEntkfvtKMYNEIL 206
|
170 180 190
....*....|....*....|....*....|
gi 1387230349 260 DYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd22196 207 ILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
140-168 |
1.99e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 42.24 E-value: 1.99e-05
10 20
....*....|....*....|....*....
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
508-694 |
2.38e-05 |
|
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: 48.47 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 508 KEKEAALCLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNS-VFEE--SDSGATKSPLHLAAYNGHHQAL 584
Cdd:cd22192 26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPmtSDLYQGETALHIAVVNQNLNLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 585 EVLLQSLVDLD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVINGHTL- 649
Cdd:cd22192 106 RELIARGADVVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVLQPNKTf 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 650 -C----MRLLLEIADNPEVVD-VKDAKGQTPLMLAVAYGHSDAVSLLLEKE 694
Cdd:cd22192 185 aCqmydLILSYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
645-784 |
2.66e-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: 48.22 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 645 NGHTLCMRLLLEIADN-PEVVDV---------------------KDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDA--- 699
Cdd:cd22194 93 TGKTCLMKALLNINENtKEIVRIllafaeengildrfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhak 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 700 ------VDIMGC-----TALHRGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELLQMAL- 761
Cdd:cd22194 173 gvffnpKYKHEGfyfgeTPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILl 252
|
170 180
....*....|....*....|....*.
gi 1387230349 762 ---SEEDCSFKDNQGYTPLHWACYNG 784
Cdd:cd22194 253 kseNKNLETIRNNEGLTPLQLAAKMG 278
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
93-147 |
2.82e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
132-180 |
2.90e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1387230349 132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
839-954 |
2.97e-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: 48.22 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 839 KGRTPLHAAAFADHVECLQLLLRHNAQVNAADNS--------------GKTPLMMAAENGQAGAVDILVNSAQADLTVKD 904
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 905 KDLNTSLHL-----ASSKGHEKCALLILDKI----QDESLINAKNNALQTPLHVAARNG 954
Cdd:cd22194 220 SRGNTVLHAlvtvaEDSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
332-577 |
3.02e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 48.15 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870 45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 403 ----------KFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIETLV 458
Cdd:TIGR00870 116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 459 TTGASVNETDDWGRTALHYaaasdmdrkSKIILGNAHENSE-----------ELERARELKEkeaalcLEFLLQHDANPS 527
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHL---------LVMENEFKAEYEElscqmynfalsLLDKLRDSKE------LEVILNHQGLTP 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 528 --IRDKEGYNSIhyaaayghrqcLELLLERTNSV--FEESdsgaTKSPLHLAAY 577
Cdd:TIGR00870 261 lkLAAKEGRIVL-----------FRLKLAIKYKQkkFVAW----PNGQQLLSLY 299
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
601-655 |
3.10e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.10e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1387230349 601 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCMRLLL 655
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
29-81 |
3.30e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.30e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 29 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857 4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
853-989 |
3.42e-05 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 47.71 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 853 VECLQLLLRHNAQVNAADNSGKTPLMMAAENGQ---AGAVDILVNsAQADLTVKDKDLNTSLHL-ASSKGHEKCALLILD 928
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLE-AGADVNAPERCGFTPLHLyLYNATTLDVIKLLIK 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 929 KIQDeslINAKNNALQTPLHVAARnGLKV---VVEELLAKGACVLAVDENGHTPALACAPNKDV 989
Cdd:PHA03095 106 AGAD---VNAKDKVGRTPLHVYLS-GFNInpkVIRLLLRKGADVNALDLYGMTPLAVLLKSRNA 165
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
875-969 |
3.63e-05 |
|
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: 47.70 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 875 TPLMMAAENGQAGAVDILVNSAQADLTVKDKDLNTSLHLASSKGHEKCALLILDkiQDESLIN-AKNNAL---QTPLHVA 950
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
|
90
....*....|....*....
gi 1387230349 951 ARNGLKVVVEELLAKGACV 969
Cdd:cd22192 97 VVNQNLNLVRELIARGADV 115
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
827-880 |
3.75e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 3.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1387230349 827 AIDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMA 880
Cdd:pfam13857 3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
839-871 |
4.96e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.12 E-value: 4.96e-05
10 20 30
....*....|....*....|....*....|....
gi 1387230349 839 KGRTPLHAAA-FADHVECLQLLLRHNAQVNAADN 871
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
423-478 |
6.24e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 6.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 423 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYA 478
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
607-691 |
7.44e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 607 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCMRLLLEIADNPEVVDvKDakGQTPLMLAVAYGHSDA 686
Cdd:PTZ00322 89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163
|
....*
gi 1387230349 687 VSLLL 691
Cdd:PTZ00322 164 VQLLS 168
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
140-280 |
7.59e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 46.68 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLVNHGAE-VTCKDK 204
Cdd:cd22194 141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEInvygntalHLACYNgqdavvneltdygANVNQ-PNNSGFTPLHF 278
Cdd:cd22194 221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMI--------LLKSEN-------------KNLETiRNNEGLTPLQL 273
|
..
gi 1387230349 279 AA 280
Cdd:cd22194 274 AA 275
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
258-312 |
8.81e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 8.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 258 LTDYGANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
344-438 |
9.28e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 344 HVAARyGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKL 423
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
90
....*....|....*
gi 1387230349 424 LQSSGADFHKKDKCG 438
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
405-555 |
1.03e-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: 46.39 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 405 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ASVNETD 468
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 469 DWGRTALHYAAasdmdrkskIILGNAHENSEELERA-RELKEKEAALCLEFLLQhdanpSIRDKEGYNSIHYAAAYGHRQ 547
Cdd:cd22197 174 SLGNTVLHALV---------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIE 239
|
....*...
gi 1387230349 548 CLELLLER 555
Cdd:cd22197 240 IFRHILQR 247
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
657-709 |
1.06e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 657 IADNPEVVDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALH 709
Cdd:pfam13857 2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
645-724 |
1.12e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 645 NGHTLCMRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 724
Cdd:PTZ00322 92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
211-314 |
1.15e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322 88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
|
90 100 110
....*....|....*....|....*....|....*..
gi 1387230349 291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322 166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
310-404 |
1.21e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322 79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
90 100
....*....|....*....|....*...
gi 1387230349 383 AHSDCCRKLLS---SGFEIDT---PDKF 404
Cdd:PTZ00322 159 GFREVVQLLSRhsqCHFELGAnakPDSF 186
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
614-883 |
1.27e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 45.98 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 614 TECVEALINQGASIFVKDNvTKRTPLHASVIN----GHTLCMRLLLeIADNPEVvDVKDAKGQTPL--MLAVAYGHS-DA 686
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDN-EYSTPLCTILSNikdyKHMLDIVKIL-IENGADI-NKKNSDGETPLycLLSNGYINNlEI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 687 VSLLLEKEANVDAVDIMGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqmalse 763
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK----------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 764 edcsfkdnQGYTPLHwaCY-NGNENCIEV-LLEQKCFRTFIGNPFTPLH--------CAIINDHENCASLLLGAIDSSI- 832
Cdd:PHA02798 181 --------EKYDTLH--CYfKYNIDRIDAdILKLFVDNGFIINKENKSHkkkfmeylNSLLYDNKRFKKNILDFIFSYId 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 833 VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTPLMMAAEN 883
Cdd:PHA02798 251 INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
858-914 |
1.33e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387230349 858 LLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLA 914
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
161-347 |
1.37e-04 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 45.84 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 161 AKGANINAFDKKDRRALHWAAYMG-HLDVVALLVNHGAEVtckdKKGYTPLHAAaSNGQINVVKHLLNLGVEIDEinvyG 239
Cdd:TIGR00870 40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAI-SLEYVDAVEAILLHLLAAFR----K 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 240 NTALHLAcyNGQDavvneLTDYGAnvnqpnnsGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVH 316
Cdd:TIGR00870 111 SGPLELA--NDQY-----TSEFTP--------GITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387230349 317 GRFTRS-----------QTLIQNGGEIDCVDKDGNTPLHVAA 347
Cdd:TIGR00870 175 GESPLNaaaclgspsivALLSEDPADILTADSLGNTLLHLLV 216
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
515-553 |
1.40e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.72 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1387230349 515 CLEFLLQHDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 553
Cdd:pfam13637 16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
636-691 |
1.57e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 636 RTPLHASVINGHTLCMRLLLEiadNPEVVDVKDAKGQTPLMLAVAYGHSDAVSLLL 691
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
205-234 |
2.14e-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: 39.49 E-value: 2.14e-04
10 20 30
....*....|....*....|....*....|
gi 1387230349 205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
272-304 |
2.39e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.19 E-value: 2.39e-04
10 20 30
....*....|....*....|....*....|...
gi 1387230349 272 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023 2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
851-986 |
2.58e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 45.05 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 851 DHVECLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVnSAQADLTVKDKDLNTSLHLASSKGH----------- 919
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL-SYGADVNIIALDDLSVLECAVDSKNidtikaiidnr 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 920 ---EKCALLILDKIQDESL------------INAKNNALQTPLHVAARN-GLKVVVEELLAKGACVLAVDENGHTPALAC 983
Cdd:PHA02876 235 sniNKNDLSLLKAIRNEDLetslllydagfsVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
|
...
gi 1387230349 984 APN 986
Cdd:PHA02876 315 AKN 317
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
236-313 |
3.16e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 44.20 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 236 NVYGNTALHLACYNGQDAVVNeLTDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884 68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
841-1052 |
3.41e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.21 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 841 RTPLHAAAFADHVECLQLLLRHNAQVN-AADNSGKTPLMMAAENGQAGAVDILVnSAQADLTVKDKDLNTSLHLASSKGH 919
Cdd:PHA02875 69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 920 EKCALLILDKiqdESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALIL-- 997
Cdd:PHA02875 148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIkr 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 998 ---ATMMTFSPSSTMTAVNFVCFKKDSLSRTTLSNLGS--MVSLCSNNVGSEDGYNENDS 1052
Cdd:PHA02875 225 gadCNIMFMIEGEECTILDMICNMCTNLESEAIDALIAdiAIRIHKKTIRRDEGFKNNMS 284
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
238-266 |
3.49e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 3.49e-04
10 20
....*....|....*....|....*....
gi 1387230349 238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
845-938 |
3.73e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 845 HAAAFADHVEcLQLLLRHNAQVNAADNSGKTPLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTSLHLASSKGHEKCAL 924
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
|
90
....*....|....
gi 1387230349 925 LILDKIQDESLINA 938
Cdd:PTZ00322 166 LLSRHSQCHFELGA 179
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
570-608 |
3.74e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.74e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1387230349 570 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 608
Cdd:pfam13857 18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
236-279 |
4.05e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 4.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1387230349 236 NVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFA 279
Cdd:pfam13857 13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
676-768 |
4.13e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 676 MLAV------AYGHSDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 747
Cdd:PTZ00322 81 MLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158
|
90 100
....*....|....*....|.
gi 1387230349 748 GhatwLSELLQMALSEEDCSF 768
Cdd:PTZ00322 159 G----FREVVQLLSRHSQCHF 175
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
670-701 |
4.61e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.42 E-value: 4.61e-04
10 20 30
....*....|....*....|....*....|...
gi 1387230349 670 KGQTPLMLAVA-YGHSDAVSLLLEKEANVDAVD 701
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
55-227 |
5.87e-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: 43.98 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 55 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 122
Cdd:cd22194 111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 123 aeviipllssvnvSDRG---GRTALHHAALNGHVEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 189
Cdd:cd22194 181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1387230349 190 --ALLVNHGAEV--TCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:cd22194 247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
213-350 |
5.87e-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: 43.98 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVN--------QP--NNSGF----TPLHF 278
Cdd:cd22194 120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194 195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272
|
....*.
gi 1387230349 345 VAARYG 350
Cdd:cd22194 273 LAAKMG 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
274-326 |
6.11e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 6.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
376-476 |
6.56e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.72 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 376 LHLAALNAHS---DCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGADFH--------K 433
Cdd:cd21882 30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSaratgrffR 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1387230349 434 KDKC-----GRTPLHYAAANCHFHCIETLVTTG---ASVNETDDWGRTALH 476
Cdd:cd21882 110 KSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
689-744 |
6.95e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 6.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 689 LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 744
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
214-360 |
7.05e-04 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 43.75 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDAVVNELTDYGANVNQPNNSGFTPLHfaaaSTHGALCLEL 291
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 292 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPLH----VAARYGHELLINTLIT 360
Cdd:PHA02716 368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIS 424
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
397-445 |
7.52e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 7.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1387230349 397 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
40-226 |
7.85e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 43.33 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882 72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 104 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaa 181
Cdd:cd21882 152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1387230349 182 ymgHLDVVALLVNHgaevtckdkKGYTPLHAAASNGQINVVKHLL 226
Cdd:cd21882 192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
205-234 |
9.15e-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: 37.62 E-value: 9.15e-04
10 20 30
....*....|....*....|....*....|
gi 1387230349 205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
238-270 |
9.18e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.65 E-value: 9.18e-04
10 20 30
....*....|....*....|....*....|....
gi 1387230349 238 YGNTALHLACY-NGQDAVVNELTDYGANVNQPNN 270
Cdd:pfam00023 1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
214-478 |
9.19e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 43.19 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HLACYNGQDAVVNELTDYGANVNQpnnSGF--TPL-----HFAAAST 283
Cdd:PHA02989 11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989 86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 354 LINT-----LITSGADT-AKCGIHSMFPLHLAALNAHS----DCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV---EC 420
Cdd:PHA02989 157 SVKKdvikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFLDNNKIlskKE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 421 IKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGASVNETDDWGRTALHYA 478
Cdd:PHA02989 237 FKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
65-114 |
9.72e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 9.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1387230349 65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
839-868 |
1.04e-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: 37.57 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|
gi 1387230349 839 KGRTPLHAAAFADHVECLQLLLRHNAQVNA 868
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
569-620 |
1.15e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.96 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 569 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 620
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
42-72 |
1.40e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 37.27 E-value: 1.40e-03
10 20 30
....*....|....*....|....*....|..
gi 1387230349 42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
140-280 |
1.63e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 42.53 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallvnhgaevtckdkkgytPLHAA 213
Cdd:cd22197 94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHLACYNGQDAVVN---------ELTDYGANVNQ-------PNNSGFT 274
Cdd:cd22197 148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227
|
....*.
gi 1387230349 275 PLHFAA 280
Cdd:cd22197 228 PLKLAA 233
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
438-469 |
1.66e-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: 36.88 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|...
gi 1387230349 438 GRTPLHYAAANC-HFHCIETLVTTGASVNETDD 469
Cdd:pfam00023 2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
438-466 |
1.71e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.71e-03
10 20
....*....|....*....|....*....
gi 1387230349 438 GRTPLHYAAANCHFHCIETLVTTGASVNE 466
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
772-794 |
1.80e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 1.80e-03
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
363-555 |
2.21e-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: 42.09 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 363 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:cd22193 26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGAD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 431 ---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVT---TGASVNETDDWGRTALHYAAAsdmdrkskiILGN 493
Cdd:cd22193 102 vhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVT---------VADN 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 494 AHENSEELERA-RELKEKEAALCLEFLLQhdanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 555
Cdd:cd22193 173 TKENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
600-632 |
2.23e-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: 36.50 E-value: 2.23e-03
10 20 30
....*....|....*....|....*....|....
gi 1387230349 600 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 632
Cdd:pfam00023 1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02795 |
PHA02795 |
ankyrin-like protein; Provisional |
124-201 |
2.31e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165157 [Multi-domain] Cd Length: 437 Bit Score: 41.52 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLVNH 195
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284
|
....*.
gi 1387230349 196 GAEVTC 201
Cdd:PHA02795 285 PLSIDC 290
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
519-575 |
2.31e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.31e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 519 LLQHD-ANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSVFEESDSGATksPLHLA 575
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLT--ALDLA 56
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
630-742 |
2.39e-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: 41.70 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 630 KDNVTKRTPLHASVIN---GHTLCMRLLLEIAD---------NPEVVDVKdAKGQTPLMLAVAYGHSDAVSLLLEKEANV 697
Cdd:cd22193 24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 698 DAVD--------------IMGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 742
Cdd:cd22193 103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
405-433 |
2.44e-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: 2.44e-03
10 20
....*....|....*....|....*....
gi 1387230349 405 GRTCLHAAAAGGNVECIKLLQSSGADFHK 433
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
338-364 |
2.47e-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: 2.47e-03
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
43-121 |
2.61e-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: 41.99 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
90
....*....|...
gi 1387230349 109 TPLHVAAANKAVK 121
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
140-282 |
2.62e-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: 41.70 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLVNHG---AEVTCK 202
Cdd:cd22193 76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHLACYNGqdavvneLTDYGANVNQP-------NNSGFTP 275
Cdd:cd22193 156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211
|
....*..
gi 1387230349 276 LHFAAAS 282
Cdd:cd22193 212 LQLAAKM 218
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
877-997 |
2.77e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 41.78 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 877 LMMAAENGQAGAVDILVNsAQADLTVKDKDLNTSLHLASSKGHEKCALLILD-----KIQDES-------LINAKNNALQ 944
Cdd:PLN03192 529 LLTVASTGNAALLEELLK-AKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKhacnvHIRDANgntalwnAISAKHHKIF 607
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387230349 945 TPLH----------------VAARNGLKVVVEELLAKGACVLAVDENGHTpALACAPNKDVADCLALIL 997
Cdd:PLN03192 608 RILYhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-318 |
3.01e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 189 VALLVNHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhlacyngqDAV-VNELTDYGANVN 266
Cdd:PTZ00322 44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1387230349 267 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
670-699 |
3.10e-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: 36.08 E-value: 3.10e-03
10 20 30
....*....|....*....|....*....|
gi 1387230349 670 KGQTPLMLAVAYGHSDAVSLLLEKEANVDA 699
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
176-204 |
3.14e-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: 3.14e-03
10 20 30
....*....|....*....|....*....|
gi 1387230349 176 ALHWAAYM-GHLDVVALLVNHGAEVTCKDK 204
Cdd:pfam00023 5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
728-780 |
3.57e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.56 E-value: 3.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1387230349 728 VSILCKDSRGRTPLHYAAARGHATWLSELLQMalsEEDCSFKDNQGYTPLHWA 780
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY---GVDLNLKDEEGLTALDLA 56
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
55-195 |
3.69e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.74 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884 47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLVNH 195
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
291-346 |
5.03e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 5.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387230349 291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
40-237 |
5.11e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 119
Cdd:PHA02791 60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 120 vkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLVNHGAE 198
Cdd:PHA02791 124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387230349 199 VTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02791 186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
153-272 |
5.43e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 39.03 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLVNHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743 37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1387230349 228 LGVEIDEINVYGNTALHLAcYNGQDAVVNE-LTDYGANVNQPNNSG 272
Cdd:PHA02743 117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
144-275 |
6.10e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLVNHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791 65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387230349 223 KHLLNlgveidEINVYGNTALHLACY-----NGQDAVVNELTDYGANVNQPNNSGFTP 275
Cdd:PHA02791 145 SYFLS------EIPSTFDLAILLSCIhitikNGHVDMMILLLDYMTSTNTNNSLLFIP 196
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
76-105 |
6.84e-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: 35.34 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|.
gi 1387230349 76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
405-436 |
6.84e-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: 35.34 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|...
gi 1387230349 405 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 436
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
76-226 |
6.95e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 40.22 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 76 TPLHRAVASRSEEAVQVLIKHSADVNAR------DKNWQT-------PLHVAAANKAVkcaEVIIPLL------SSVNVS 136
Cdd:cd22197 96 SALHIAIEKRSLQCVKLLVENGADVHARacgrffQKKQGTcfyfgelPLSLAACTKQW---DVVNYLLenphqpASLQAQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 137 DRGGRTALH-------HAALNGH--VEMVNLLLAKGANINAFDKKDRralhwaaymghldvvalLVNHgaevtckdkKGY 207
Cdd:cd22197 173 DSLGNTVLHalvmiadNSPENSAlvIKMYDGLLQAGARLCPTVQLEE-----------------ISNH---------EGL 226
|
170
....*....|....*....
gi 1387230349 208 TPLHAAASNGQINVVKHLL 226
Cdd:cd22197 227 TPLKLAAKEGKIEIFRHIL 245
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
600-629 |
7.20e-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: 34.87 E-value: 7.20e-03
10 20 30
....*....|....*....|....*....|
gi 1387230349 600 KGRTALDLAAFKGHTECVEALINQGASIFV 629
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
176-201 |
7.64e-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: 34.87 E-value: 7.64e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
238-266 |
7.88e-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: 34.93 E-value: 7.88e-03
10 20
....*....|....*....|....*....
gi 1387230349 238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
935-979 |
9.01e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.40 E-value: 9.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1387230349 935 LINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTP 979
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
385-555 |
9.20e-03 |
|
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: 40.13 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 385 SDCCRKLLSSGFEidTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCH 450
Cdd:cd22194 123 NGILDRFINAEYT--EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQ 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387230349 451 FHCIETLVTTGAS-VNETDDWGRTALH--YAAASDMDRKSKIILgnahENSEELERARELKEKEAalclefllqhdanps 527
Cdd:cd22194 201 PEIVQLLMEKESTdITSQDSRGNTVLHalVTVAEDSKTQNDFVK----RMYDMILLKSENKNLET--------------- 261
|
170 180
....*....|....*....|....*...
gi 1387230349 528 IRDKEGYNSIHYAAAYGHRQCLELLLER 555
Cdd:cd22194 262 IRNNEGLTPLQLAAKMGKAEILKYILSR 289
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
908-954 |
9.64e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 35.33 E-value: 9.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1387230349 908 NTSLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNG 954
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
|
|
| |
