NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1333587291|ref|XP_023478047|]
View 

serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X7 [Equus caballus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 7.84e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 2.97e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250       260       270
                  ....*....|....*....|....*....|
gi 1333587291 749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-934 2.08e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666   143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260
                  ....*....|....*....|....*..
gi 1333587291 908 ILVNsAQADLTVKDKDLNTPLHLASSK 934
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAEN 229
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 212-493 3.48e-25

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 110.11  E-value: 3.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095  243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.14e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291  10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 7.84e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 1.20e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 150.56  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  22 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 176 ALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHLACYN 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 250 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 2.97e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250       260       270
                  ....*....|....*....|....*....|
gi 1333587291 749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-934 2.08e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666   143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260
                  ....*....|....*....|....*..
gi 1333587291 908 ILVNsAQADLTVKDKDLNTPLHLASSK 934
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAEN 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 3.48e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 110.11  E-value: 3.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095  243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 7.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1333587291 224 HLLNLGVEIDEIN 236
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-682 1.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 397 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 474
Cdd:PHA03100    9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 475 ---LVTTGANVNETDDWGRTALHYAAAsdmdrnktilgnahenseelerarelKEKEAASCLEFLLQNEANPSIRDKEGY 551
Cdd:PHA03100   89 vklLLEYGANVNAPDNNGITPLLYAIS--------------------------KKSNSYSIVEYLLDNGANVNIKNSDGE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 552 NSIHYAAAYGHR--QCLELLLERTNsgfedsdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 629
Cdd:PHA03100  143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 630 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 682
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-931 1.30e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQIALSEEDCsfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 816 REFIGNpfTPLH--CAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQL--LLRHNAQVNAADNSGK 891
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1333587291 892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 2.31e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1333587291 702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 3.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 794 LHWACYNGNENCIEVLLEQKC-FREFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 872
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1333587291 873 LQLLLRHNAQVNAAD 887
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.10e-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: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLITHGAEVTCKDKKGYTPLH 211
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 281
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 3.53e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.53e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASD 500
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 9.84e-11

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 65.87  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 177 ---LHWAAYMGHLDVVALLITHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHLACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333587291 254 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-775 7.53e-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: 59.64  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALINqGASIFVKDNVTK-----RTPLHA 658
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 659 SVINGHTLCLRLLLEI-AD--NPEVVD---VKDAK-----GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHR 727
Cdd:cd22192    96 AVVNQNLNLVRELIARgADvvSPRATGtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 728 GIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 775
Cdd:cd22192   176 LVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-494 1.76e-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: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 340 NTPLHVAARYGHELLINTLITS-GADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 419 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:cd22192    89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|
gi 1333587291 485 TDDWGRTALH 494
Cdd:cd22192   165 QDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 587-831 1.14e-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: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 654 TPLHASVINGHTLCLRLLLEIADNPEV----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 723 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQIALSEEDCSFKDNQGYTPLHWACYNGN 802
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                         250       260       270
                  ....*....|....*....|....*....|
gi 1333587291 803 ENCIEVLLEQKCF-REFIGNPFTPLHCAII 831
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291  10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 3.05e-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: 44.50  E-value: 3.05e-06
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 738-900 5.01e-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: 50.46  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQialseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 814 CFREFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1333587291 868 DHVECLQLLLRHNAQVNAADNSGKTALMMAAEN 900
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 792-930 2.99e-04

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: 44.62  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 792 TPLHWACYNGNENCIEVLLEQK----CFREFIGNpfTPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTPLHA 863
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 864 AAFADHVECLQLLLRHNAQVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH 174


                  .
gi 1333587291 930 L 930
Cdd:cd22192   175 I 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 456-484 5.32e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 5.32e-04
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  456 GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 856-885 8.28e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.28e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  856 KGRTPLHAAAFADHVECLQLLLRHNAQVNA 885
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 687-716 2.37e-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: 2.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 3.31e-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: 41.22  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgvhsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870 116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                         170       180
                  ....*....|....*....|....*
gi 1333587291 470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 7.84e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 7.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 4.12e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 4.12e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 171 KKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNG 250
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 1333587291 251 QDAVVNELTDYGANVNQPNNSGFTPL 276
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 6.31e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.53  E-value: 6.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 182 YMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1333587291 262 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-243 1.06e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.98  E-value: 1.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291   1 MAVLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHR 80
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  81 AVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 161 AKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN 240
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                  ...
gi 1333587291 241 TAL 243
Cdd:COG0666   287 TLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 1.20e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 150.56  E-value: 1.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  22 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 176 ALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHLACYN 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 250 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 2.33e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 149.79  E-value: 2.33e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 236 NVYGNTALHLACYNGQD--AVVNELTDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1333587291 313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095  264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 2.97e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250       260       270
                  ....*....|....*....|....*....|
gi 1333587291 749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-813 2.32e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 613 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpevVDVKDAKGQTP 691
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 771
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1333587291 772 ELLQIALSEEDcsfKDNQGYTPLHWACYNGNENCIEVLLEQK 813
Cdd:COG0666   237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-301 2.86e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 142.50  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLITHGAEVTCKDKk 205
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHG 285
Cdd:PHA03100  175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                         250
                  ....*....|....*.
gi 1333587291 286 ALcLELLVNNGADVNI 301
Cdd:PHA03100  239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-525 8.95e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 8.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgvhsmfplhlaalnahsdccrkll 392
Cdd:COG0666   150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 393 ssgqkysivslfsnehvlsagfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCI 472
Cdd:COG0666   179 -----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 473 ETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERARELK 525
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-364 3.73e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 140.20  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  26 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876  243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 185 H-LDVVALLITHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PHA02876  319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 263 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876  399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                         330       340
                  ....*....|....*....|...
gi 1333587291 342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876  479 PLLIA--LEYHGIVNILLHYGAE 499
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
636-931 8.94e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 8.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 636 ALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 715
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 716 AVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLH 795
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 796 WACYNGNENCIEVLLEQkcfrefignpftplhcaiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQL 875
Cdd:COG0666   159 LAAANGNLEIVKLLLEA------------------------------GAD----VNARDNDGETPLHLAAENGHLEIVKL 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 876 LLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
600-926 1.34e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 600 ALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNpe 679
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 680 vVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLH 759
Cdd:COG0666    80 -INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 760 YAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplhcaiindhencas 839
Cdd:COG0666   159 LAAANGNLEIVKLLLE---AGADVNARDNDGETPLHLAAENGHLEIVKLLLEA--------------------------- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 840 lllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTV 919
Cdd:COG0666   209 ---GAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                  ....*..
gi 1333587291 920 KDKDLNT 926
Cdd:COG0666   282 LLDLLTL 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 5.75e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 133.17  E-value: 5.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  16 IFSGDPEEIRMLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874    9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874   89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 175 RALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAV 254
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 255 VNELTDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1333587291 333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-385 1.34e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.11  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLITHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876  240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHLACY--NGQDAVVNeLTDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                         330
                  ....*....|....*..
gi 1333587291 369 GVHSMFPLhLAALNAHS 385
Cdd:PHA02876  473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 1.46e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKC 368
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 369 GVHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 448
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 449 FHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAaasdmdrnktilgnAHENSEELerarelkeke 528
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA--------------AENGHLEI---------- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 529 aascLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSL 608
Cdd:COG0666   202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT--ALLLAAAAGAALIVKLLLLAL 275

                         330
                  ....*....|....
gi 1333587291 609 VDLDIRDEKGRTAL 622
Cdd:COG0666   276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-758 1.03e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVN 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 613 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLE-IADnpevVDVKDAKGQTP 691
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTA 222

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587291 692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPL 758
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
410-687 6.57e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 6.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 410 LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWG 489
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 490 RTALHYAAasdmdrnktilgnaHENSEELerarelkekeaascLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELL 569
Cdd:COG0666   121 ETPLHLAA--------------YNGNLEI--------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 570 LERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDN 649
Cdd:COG0666   173 LEAGADVNARDNDGET--PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333587291 650 VTKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAK 687
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-934 2.08e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666   143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260
                  ....*....|....*....|....*..
gi 1333587291 908 ILVNsAQADLTVKDKDLNTPLHLASSK 934
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAEN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-483 4.17e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 121.32  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCK 202
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ-DAVVNELTDYGANVNQPNNSGFTPLHFAAA 281
Cdd:PHA02876  241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876  317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 361 SGADtakcgvhsmfplhLAALNahsdccrkllssgqkysivslfsnehvlsagfeidtpDKFGrTCLHAAAAGGN-VECI 439
Cdd:PHA02876  397 YGAD-------------IEALS-------------------------------------QKIG-TALHFALCGTNpYMSV 425

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1333587291 440 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIETLVTTGANVN 483
Cdd:PHA02876  426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-265 1.39e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 119.78  E-value: 1.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 167 NAFDKKDRRALHWAAY-MGHLDVVALLITHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876  402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                         250       260
                  ....*....|....*....|.
gi 1333587291 245 LACynGQDAVVNELTDYGANV 265
Cdd:PHA02876  482 IAL--EYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-353 1.92e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 114.21  E-value: 1.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLITHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878  113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 226 LNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333587291 305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAA--RYGHEL 353
Cdd:PHA02878  268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-238 2.62e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 109.75  E-value: 2.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  28 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100   21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100  101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587291 172 ---------KDRR---ALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100  179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 3.48e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 110.11  E-value: 3.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095  243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-483 7.54e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 7.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 192 LITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLAC---YNGQDAV--VNELTDYGANVN 266
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 267 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100  101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 346 aaryghelLINTLITSGADtakcgvhsmfplhlaaLNAhsdCCRkllssgqkysiVSLFsnehvLSAGFEIDTPDKFGRT 425
Cdd:PHA03100  158 --------ILKLLIDKGVD----------------INA---KNR-----------VNYL-----LSYGVPINIKDVYGFT 194

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 426 CLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-295 2.40e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.50  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878   18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878   98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 229 GVEID-EINVYGNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878  258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 323-625 4.18e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 323 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 401
Cdd:PHA02874   18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 402 SL--FSNEHV---LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:PHA02874   98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 477 TTGANVNETDDWGRTALHYAAasdmdrnktilgnahenseelerarelkEKEAASCLEFLLQNEANPSIRDKEGYNSIHY 556
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAA----------------------------EYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587291 557 AAAYgHRQCLELLLerTNSGFEDSD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:PHA02874  230 AIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 7.21e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1333587291 224 HLLNLGVEIDEIN 236
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-235 9.82e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 96.63  E-value: 9.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  24 IRMLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 176 ALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-682 1.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 397 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 474
Cdd:PHA03100    9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 475 ---LVTTGANVNETDDWGRTALHYAAAsdmdrnktilgnahenseelerarelKEKEAASCLEFLLQNEANPSIRDKEGY 551
Cdd:PHA03100   89 vklLLEYGANVNAPDNNGITPLLYAIS--------------------------KKSNSYSIVEYLLDNGANVNIKNSDGE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 552 NSIHYAAAYGHR--QCLELLLERTNsgfedsdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 629
Cdd:PHA03100  143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 630 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 682
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 1.68e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 177 LHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHLACYNGQDAVVN 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1333587291 257 ELTDYGANVNQPN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 192-714 3.58e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.90  E-value: 3.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 192 LITHGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYG-NTALHLACY--NGQDAVVNELTDYGANVNQ 267
Cdd:PHA02876   27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 268 PNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTLIQNGGEIDCVDKDGN 340
Cdd:PHA02876  106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCI 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 341 TPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSIVSLFSNEH------V 409
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSLLKAIRNEDletsllL 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 410 LSAGFEIDTPDKFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHCIETLVTTGANVNETD 486
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 487 DWGRTALHyaAASDMDRNKTILGNahenseelerarelkekeaasclefLLQNEANPSIRDKEGYNSIHYAAAYGHRQCL 566
Cdd:PHA02876  339 RLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 567 ELLLertnsgfedsDSGAtksplhlaaynghhqalevllqslvDLDIRDEKGRTALDLAAFKGHT-ECVEALINQGASIF 645
Cdd:PHA02876  392 NTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVN 436

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 646 VKdNVTKRTPLHASVINGHTL-CLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLEKEANV 714
Cdd:PHA02876  437 SK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-266 1.02e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 92.75  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKG 206
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587291 207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHLACYNGQDAVVNELTDYGANVN 266
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-463 2.22e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.95  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 150 NGHVEMV-NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNL 228
Cdd:PHA02874   11 SGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 229 GVEideinvygNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASthGAL-CLELLVNNGADVNIQSKDGK 307
Cdd:PHA02874   91 GVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNGC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD-TAKCGvHSMFPLHLAALnahsd 386
Cdd:PHA02874  159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHiMNKCK-NGFTPLHNAII----- 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 387 ccrkllssgQKYSIVSLFSNEHvlsagfEIDTPDKFGRTCLH-AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02874  233 ---------HNRSAIELLINNA------SINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 410-718 2.87e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 2.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 410 LSAGFEIDTPDKFGRTCLHAAAAGGNVEC---IKLLQSSGADFHKKDKCGRTPLH-YAAANCHFHCIETLVTTGANVNET 485
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAK 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 486 DDWGRTALH-YAaasdmdRNKTIlgnahenseelerarelkekeAASCLEFLLQNEANPSIRDKEGYNSIHyaAAYGHRQ 564
Cdd:PHA03095  114 DKVGRTPLHvYL------SGFNI---------------------NPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 565 C----LELLLERTNSGFEDSDSGatKSPLHLAAYNGHHQA--LEVLLQSLVDLDIRDEKGRTALDLAAFkgHTEC----V 634
Cdd:PHA03095  165 AnvelLRLLIDAGADVYAVDDRF--RSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCkrslV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 635 EALINQGASIFVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEAN 713
Cdd:PHA03095  241 LPLLIAGISINARNRYGQ-TPLHyAAVFNNPRACRRLIALGAD----INAVSSDGNTPLSLMVRNNNGRAVRAALAKNPS 315


                  ....*
gi 1333587291 714 VDAVD 718
Cdd:PHA03095  316 AETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 3.02e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1333587291 191 LLITHGAEVTCKD 203
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-864 1.25e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.64  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 589 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 666
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 667 CLRLLLE--------------------IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 726
Cdd:PHA02874   83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 727 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNgNENCI 806
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 807 EVLLEQKCFREFIGNPFTPLHCAIIN--DHENCASLLLGAIDSSIvncRDDKGRTPLHAA 864
Cdd:PHA02874  239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-931 1.30e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQIALSEEDCsfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 816 REFIGNpfTPLH--CAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQL--LLRHNAQVNAADNSGK 891
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1333587291 892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 2.31e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1333587291 702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 155-616 7.68e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.58  E-value: 7.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 155 MVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 235 -----INVYGNTALHLACYngqdavvneLTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSP 309
Cdd:PHA02876  240 ndlslLKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 310 LHMTAVHGRFTRS-QTLIQNGGEIDCVDKDGNTPLHVAAryghellintlitsgadtakcgvhsmfplhlaalnahsdcc 388
Cdd:PHA02876  311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAS----------------------------------------- 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 389 rkllssgqkysivslfsnehvlsagfeidTPDKFGRTClhaaaaggnvecIKLLQSsGADFHKKDKCGRTPLHYAAANCH 468
Cdd:PHA02876  350 -----------------------------TLDRNKDIV------------ITLLEL-GANVNARDYCDKTPIHYAAVRNN 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 469 FHCIETLVTTGANVNETDDWGRTALHYAAASD---MDRNKTILGNAHENSEELERARELKEKEAASC----LEFLLQNEA 541
Cdd:PHA02876  388 VVIINTLLDYGADIEALSQKIGTALHFALCGTnpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCkldvIEMLLDNGA 467

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333587291 542 NPSIRDKEgyNSIHYAAAYGHRQCLELLLertNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDE 616
Cdd:PHA02876  468 DVNAINIQ--NQYPLLIALEYHGIVNILL---HYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNE 537
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 8.43e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 8.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1333587291 125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 3.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 794 LHWACYNGNENCIEVLLEQKC-FREFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 872
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1333587291 873 LQLLLRHNAQVNAAD 887
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 3.81e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 668
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1333587291 669 RLLLEIADNPEVVD 682
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-751 1.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 656 LHASVINGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDAVDiMGCTALHRGIMTGHEE 735
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA---NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 1333587291 736 CVQMLLEQEVSILCKD 751
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 1.56e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1333587291  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 2.10e-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: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLITHGAEVTCKDKKGYTPLH 211
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 281
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 533-743 2.22e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.73  E-value: 2.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 610
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 611 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEVVDVKDAKGQT 690
Cdd:PHA02875   96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 691 PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC-TALHRGIMTGHEECVQMLLEQ 743
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-170 3.34e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.62  E-value: 3.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  20 DPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291  99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878  226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 634-907 3.63e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 634 VEALINQGASIFVKDNVtKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEA 712
Cdd:PHA03095   30 VRRLLAAGADVNFRGEY-GKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 713 NVDAVDIMGCTALH---RGiMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATwlSELLQIALSE-EDCSFKDN 788
Cdd:PHA03095  109 DVNAKDKVGRTPLHvylSG-FNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAN--VELLRLLIDAgADVYAVDD 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 789 QGYTPLHWAC--YNGNENCIEVLLEQKC---FREFIGNpfTPLHCAIIndHENCASLLLGA--IDSSIVNCRDDKGRTPL 861
Cdd:PHA03095  186 RFRSLLHHHLqsFKPRARIVRELIRAGCdpaATDMLGN--TPLHSMAT--GSSCKRSLVLPllIAGISINARNRYGQTPL 261

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1333587291 862 H-AAAFADHVECLQLLlRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:PHA03095  262 HyAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
725-814 4.39e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 725 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAtwlsELLQIALSEEDCSFKDNqGYTPLHWACYNGNEN 804
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 1333587291 805 CIEVLLEQKC 814
Cdd:pfam12796  76 IVKLLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 6.92e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 6.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  17 FSGDPEEIRMLIHKTEDVNALDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                  .
gi 1333587291 168 A 168
Cdd:PHA03095  285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-648 1.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 554 IHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 633
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1333587291 634 VEALINQGASIFVKD 648
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-364 1.96e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 80.26  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798   44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798   94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 232 IDEI-NVYGNTALHlaCY-----NGQDA-VVNELTDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798  174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798  244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 3.53e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 3.53e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASD 500
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 8.81e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 8.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 376 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 455
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1333587291 456 GRTPLHYAAANCHFHCIETLVTTGANVNETD 486
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 585-926 9.21e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 9.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 585 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 648
Cdd:PHA02876  178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 649 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEVVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 714
Cdd:PHA02876  258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 715 DAVDIMGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIALSEEDCSFKDNqgyTP 793
Cdd:PHA02876  335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 794 LHWACYNGNencievlleqkcfrefignPFTPLHcAIINDHENcaslllgaidssiVNCRDDKGRTPLHAAAFAD-HVEC 872
Cdd:PHA02876  412 LHFALCGTN-------------------PYMSVK-TLIDRGAN-------------VNSKNKDLSTPLHYACKKNcKLDV 458

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 873 LQLLLRHNAQVNAADNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNT 926
Cdd:PHA02876  459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLND 512
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-167 9.86e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 9.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291   9 QPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228


                  .
gi 1333587291 167 N 167
Cdd:PHA02875  229 N 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
692-766 9.91e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 9.91e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333587291 692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 766
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
Ank_2 pfam12796
Ankyrin repeats (3 copies);
826-921 1.76e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 826 LHCAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQLLLRHnAQVNAADNsGKTALMMAAENGQAGA 905
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD--ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*.
gi 1333587291 906 VDILVNSAqADLTVKD 921
Cdd:pfam12796  77 VKLLLEKG-ADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 567-749 2.92e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.22  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 567 ELLLERTnsgfEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:PLN03192  511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 647 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTA 724
Cdd:PLN03192  587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         170       180
                  ....*....|....*....|....*
gi 1333587291 725 LHRGIMTGHEECVQMLLEQEVSILC 749
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
758-842 3.84e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 758 LHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFREFiGNPFTPLHCAIINDHENC 837
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76


                  ....*
gi 1333587291 838 ASLLL 842
Cdd:pfam12796  77 VKLLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 173-408 1.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 173 DRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVeIDEINVYG-NTALHLACYNGQ 251
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 252 DAVVNELTDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 330
Cdd:PHA02875   81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587291 331 EIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 408
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 602-945 1.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 602 EVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 679
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 680 VVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH-EECVQMLLEQEVSILC 749
Cdd:PHA02876  223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 750 KDSRGRTPLHYAAARGHATwlSELLQIALSEEDCSFKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrefignpftplhc 828
Cdd:PHA02876  303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 829 aiindhencasllLGAidssIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMA-AENGQAGAVD 907
Cdd:PHA02876  364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1333587291 908 ILVNSAqADLTVKDKDLNTPLHLASSKppaRCCPQRLE 945
Cdd:PHA02876  427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIE 460
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 656-926 2.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 656 LHASVINGHTLCLRLLLE--IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH 733
Cdd:PHA03100    1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 734 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQIALseeDCSFKDNQGYTPLHWA--CYNGNEN 804
Cdd:PHA03100   81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 805 CIEVLLEqkcfrefignpftplHCAIINDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVN 884
Cdd:PHA03100  158 ILKLLID---------------KGVDINAKNRVNYLLSYGVP---INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1333587291 885 AADNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 926
Cdd:PHA03100  220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-201 2.87e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.13  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTC 201
Cdd:PLN03192  612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
526-615 3.47e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 526 EKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSgfEDSDSGATksPLHLAAYNGHHQALEVLL 605
Cdd:pfam12796   6 KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1333587291 606 QSLVDLDIRD 615
Cdd:pfam12796  82 EKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-273 5.14e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.56  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINA----------------------------------- 168
Cdd:PHA02798  132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkekydtlhcyfkynidridadilklfvdngfi 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 169 ---FDKKDRRALhwAAYMGHL---------DVVALLITHgAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEIN 236
Cdd:PHA02798  212 inkENKSHKKKF--MEYLNSLlydnkrfkkNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1333587291 237 VYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGF 273
Cdd:PHA02798  289 ELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 407-761 1.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.02  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetd 486
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 487 dwgrtalhyaaasdmdRNKTILGNAHENSEelerarelkekeaasclefllqneanpsirdkegynsihyaaayghrqcL 566
Cdd:PHA02876  239 ----------------KNDLSLLKAIRNED-------------------------------------------------L 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 567 ELLLERTNSGFE-DSDSGATKSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGAS 643
Cdd:PHA02876  254 ETSLLLYDAGFSvNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGAD 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 644 IFVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:PHA02876  334 VNAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1333587291 723 TALHRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:PHA02876  410 TALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-568 1.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGVHSM-FPLHLAALNA 383
Cdd:PHA02878  111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 384 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878  180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 464 AANC-HFHCIETLVTTGANVN-ETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERAREL----KEKEAASCLEFL- 536
Cdd:PHA02878  242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTPLssavKQYLCINIGRILi 321

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1333587291 537 ----LQNEANPSIRDKEGYnSIHYAAAYGHRQCLEL 568
Cdd:PHA02878  322 snicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-628 1.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGVHSmfplhlaALNAHSDC 387
Cdd:PHA02878   40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 388 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDKFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 466
Cdd:PHA02878  109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 467 CHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgnahenseelerarelkekeaascLEFLLQNEANPSIR 546
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 547 DKEGYNSIHYAAAY-GHRQCLELLLER-TNSGFEDSDSGATksPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDL 624
Cdd:PHA02878  231 DKCGNTPLHISVGYcKDYDILKLLLEHgVDVNAKSYILGLT--ALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSS 306


                  ....
gi 1333587291 625 AAFK 628
Cdd:PHA02878  307 AVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-483 2.17e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 254 VVNELTDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875   17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgvhsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 412
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587291 413 gfEIDTPDKFgrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA02875  129 --DIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 4.57e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 4.57e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-934 6.52e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 6.52e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 861 LHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLASSK 934
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARS 71
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-463 8.55e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 8.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 166 INAFDKKDRRA----------LHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878   20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 236 NVYgnTALHLACYNGQDAVVNE-LTDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 313
Cdd:PHA02878  100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 314 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADT---AKCGVHsmfPLHLAAlnahsdccrk 390
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTdarDKCGNT---PLHISV---------- 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 391 llSSGQKYSIVSLfsnehVLSAGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878  243 --GYCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-453 9.63e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 9.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 343 LHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSlfsnehvlsagfeidtpdkf 422
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-------------------- 60

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1333587291 423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 453
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 761-930 1.13e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 761 AAARGHATWLSELLQIALseeDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FREFIGNpfTPLHCAIINDHENC 837
Cdd:PLN03192  532 VASTGNAALLEELLKAKL---DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 838 ASLLLGAIDSSIVNCRDDKgrtpLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILV-NSAQAD 916
Cdd:PLN03192  607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                         170
                  ....*....|....
gi 1333587291 917 LTVKDKDLnTPLHL 930
Cdd:PLN03192  683 KANTDDDF-SPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-476 1.79e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.79e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-275 2.41e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 64.07  E-value: 2.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLITHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859   63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 224 HLLNLGVEIDEINVYGNTALH-LACYNGQDAVVNELTDYGANVNQPNNSGFTP 275
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 544-721 3.85e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 3.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 544 SIRDKEGYNSIHYAAAYGHRQCLELLLE-RTNSGFEDsDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTAL 622
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEyGADVNIED-DNGCY--PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 623 DLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGhtlclRLLLEIADNPEVVDVKDAKGQTPLMLAVAYG-HI 701
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN-----RSAIELLINNASINDQDIDGSTPLHHAINPPcDI 268

                         170       180
                  ....*....|....*....|
gi 1333587291 702 DAVSLLLEKEANVDAVDIMG 721
Cdd:PHA02874  269 DIIDILLYHKADISIKDNKG 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 5.85e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.85e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 174 RRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-336 6.26e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 243 LHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1333587291 323 QTLIQNGGEIDCVD 336
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-696 6.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 6.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 459 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH--------------------------YAAASDM--DRN----KT 506
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAfnNRNveifKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 507 ILGNAHENSEELErARELKEKEAASCLE-----FLLQNEANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERtnsGFE-D 579
Cdd:PHA02878  120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSY---GANvN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 580 SDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPLHA 658
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHS 275

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333587291 659 SVINGHTlcLRLLLEIADNPEVVdvkDAKGQTPLMLAV 696
Cdd:PHA02878  276 SIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 153-315 9.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 9.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVtcKD---KKGYTPLHAAASNGQINVVKHLLNLG 229
Cdd:PHA02875   48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA--DDvfyKDGMTPLHLATILKKLDIMKLLIARG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 230 VEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALClELLVNNGADVNIQSKDGKSP 309
Cdd:PHA02875  126 ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC-KMLLDSGANIDYFGKNGCVA 204


                  ....*.
gi 1333587291 310 LHMTAV 315
Cdd:PHA02875  205 ALCYAI 210
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 9.84e-11

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 65.87  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 177 ---LHWAAYMGHLDVVALLITHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHLACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1333587291 254 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-400 1.39e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGVHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1333587291 390 KLLSSGQKYSI 400
Cdd:pfam12796  79 LLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-114 3.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291   3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1333587291  81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878  276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 627-935 4.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 627 FKGHTECVEALI-NQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVS 705
Cdd:PHA02874   10 YSGDIEAIEKIIkNKGNCINISVDETT-TPLIDAIRSGDAKIVELFIKHGAD---INHINTKIPHPLLTAIKIGAHDIIK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 706 LLLEKEANVDAVDIMGCtalhrgimtgHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIAlseEDCSF 785
Cdd:PHA02874   86 LLIDNGVDTSILPIPCI----------EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---ADVNI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 786 KDNQGYTPLHWACYNGNENCIEVLLEQKCFrefignpftplhcaiindhencaslllgaidssiVNCRDDKGRTPLHAAA 865
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAY----------------------------------ANVKDNNGESPLHNAA 198

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 866 FADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAgAVDILVNSAQadLTVKDKDLNTPLHLASSKP 935
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINNAS--INDQDIDGSTPLHHAINPP 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-741 5.08e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.08e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 690 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 741
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-374 1.24e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 183 MGHLDVVALLITHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 263 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1333587291 343 LHVAARYGHELLINTLITSGADTAKCGVHSMF 374
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-638 1.55e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 638
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 1.78e-09

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ...
gi 1333587291 224 HLL 226
Cdd:PTZ00322  166 LLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 147-305 2.13e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQ---INVVK 223
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHhkiFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 224 HLLNLGveideiNVY-GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQ 302
Cdd:PLN03192  612 HFASIS------DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKA 684


                  ...
gi 1333587291 303 SKD 305
Cdd:PLN03192  685 NTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 653-765 3.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 653 RTPLHASVINGHTLCLRLLLEIadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTG 732
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1333587291 733 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 765
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-164 3.92e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291  98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 55-317 4.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 59.75  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  55 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 128
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 129 LLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKKDRRA---LH--WAAYMGHLDVVALLITHGAEV-TCK 202
Cdd:PHA02989  115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKT 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 203 DKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL------HLACYNGQDAVVNELTDYgANVNQPNNSG 272
Cdd:PHA02989  178 SLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKG 256

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1333587291 273 FTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG 317
Cdd:PHA02989  257 FNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 710-933 5.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 710 KEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIALseedcsfKDNQ 789
Cdd:PHA02878   26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 790 GYT--PLHWACYNGNENCIEVLLEQKCFREFignpftplhcaIINDHENCASLLLGAIDSSI----------VNCRD-DK 856
Cdd:PHA02878   99 FYTlvAIKDAFNNRNVEIFKIILTNRYKNIQ-----------TIDLVYIDKKSKDDIIEAEItklllsygadINMKDrHK 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587291 857 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLASS 933
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVG 243
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-775 7.53e-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: 59.64  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALINqGASIFVKDNVTK-----RTPLHA 658
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 659 SVINGHTLCLRLLLEI-AD--NPEVVD---VKDAK-----GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHR 727
Cdd:cd22192    96 AVVNQNLNLVRELIARgADvvSPRATGtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 728 GIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 775
Cdd:cd22192   176 LVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 689-910 8.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 8.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 689 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 768
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 769 WLSELLQIALSEEDCSFKDnqGYTPLHWACYNGNENCIEVLLEQKCFREFIG-NPFTPLHCAIINDHENCASLLLGaiDS 847
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGDIKGIELLID--HK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 848 SIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALM-MAAENGQAGAVDILV 910
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 620-802 1.01e-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: 58.87  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 620 TALDLAAFKGHTECVEALI-NQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIAdnPEVVDVKDA----KGQTPLML 694
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 695 AVAYGHIDAVSLLLEKEANVDAVDIMGcTALHRGI---------------MTGHEECVQMLLEQEVSILCKDSRGRTPLH 759
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291 760 YAAARGHATWLSELLQIALS--EEDCS-----FKDNQGYTPLHWACYNGN 802
Cdd:cd22192   175 ILVLQPNKTFACQMYDLILSydKEDDLqpldlVPNNQGLTPFKLAAKEGN 224
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 587-757 1.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 664
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 665 TLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQE 744
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                         170
                  ....*....|...
gi 1333587291 745 VSIlckDSRGRTP 757
Cdd:PHA02875  192 ANI---DYFGKNG 201
PHA02946 PHA02946
ankyin-like protein; Provisional
 53-312 1.22e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallithgaevTCKDKKGYTPLHA 212
Cdd:PHA02946  121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946  148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226

                         250       260
                  ....*....|....*....|..
gi 1333587291 291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946  227 NLLLPSTDVNKQNKFGDSPLTL 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-147 1.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.44  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333587291  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 ...
 206-359 1.43e-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: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 206 GYTPLHAAASNGQINVVKHLLNLGVEIdeINV------Y-GNTALHLACYNGQDAVVNELTDYGANVNQPNNSG--FT-- 274
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdlYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpg 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 275 ----------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI---------QNGGEIDCV 335
Cdd:cd22192   129 pknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYdlilsydkeDDLQPLDLV 207

                         170       180
                  ....*....|....*....|....*
gi 1333587291 336 -DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192   208 pNNQGLTPFKLAAKEGNIVMFQHLV 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-644 1.68e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 429 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 508
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 509 gnahenseelerarelkekeaasclefllqneanpsirdkegynsIHYAAAyghrqclelllertnsgfedSDSGATKSP 588
Cdd:PLN03192  611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 644
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-494 1.76e-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: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 340 NTPLHVAARYGHELLINTLITS-GADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 419 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:cd22192    89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|
gi 1333587291 485 TDDWGRTALH 494
Cdd:cd22192   165 QDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
456-498 1.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1333587291 456 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 498
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 45-326 2.05e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 58.38  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  45 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 118
Cdd:PHA02716  181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 119 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 159
Cdd:PHA02716  259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 160 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQ----- 218
Cdd:PHA02716  339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 219 -----------INVVKH--LLNLGVEIDEinvyGNTALH--LACYN-GQDAVVNELTDYG----------ANVNQPNN-- 270
Cdd:PHA02716  417 diidclisdkvLNMVKHriLQDLLIRVDD----TPCIIHhiIAKYNiPTDLYTDEYEPYDstkihdvyhcAIIERYNNav 492

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 271 ---SGFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716  493 cetSGMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-250 2.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.60  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859  101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                         170       180
                  ....*....|....*....|....*
gi 1333587291 226 LNLGVEIDEINVYGNTALHLACYNG 250
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDLIKFRN 203
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 108-282 3.09e-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: 57.58  E-value: 3.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 169 FDKKDRR--------ALHWAAYMGHLDVVALLITHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882   107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 238 YGNTALHLACYNGqdavvneLTDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd21882   170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 3.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-461 3.27e-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: 57.33  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 348 RYGHELLINTLITSGADTAK---CGvhSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 424
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1333587291 425 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 461
Cdd:cd22192   143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 3.96e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291  74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 323-571 4.17e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.60  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 323 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHL-------------------AALNA 383
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 384 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 459
Cdd:PHA02946  136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 460 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHENSEELERARELKEKEAASCLeFLLQ 538
Cdd:PHA02946  212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1333587291 539 NEANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 571
Cdd:PHA02946  283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 6.99e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ....*.
gi 1333587291  92 VLIKHS 97
Cdd:PTZ00322  166 LLSRHS 171
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 11-171 7.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.05  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  11 PLVQAIFSGDPEEIRMLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859   99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                         170
                  ....*....|....
gi 1333587291 158 LLLAKGANINAFDK 171
Cdd:PHA02859  177 FLTSLGIDINETNK 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-345 8.99e-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: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGAN-VNQPNNS----GFTPLHFAAA 281
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV 345
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 840-916 1.04e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587291 840 LLLGAIDSsivNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQAD 916
Cdd:PTZ00322  101 LLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 7-114 1.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291   7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110
                  ....*....|....*....|....*....|
gi 1333587291  86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
857-910 1.34e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 857 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILV 910
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 1.73e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
723-766 1.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.76e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1333587291 723 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 766
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-251 2.16e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.16e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1333587291 206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ 251
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-261 2.50e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.50e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 189 VALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 3.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291  42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-198 3.64e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322   56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291 149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAE 198
Cdd:PTZ00322  124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 3.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.71e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 192 LITHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 325-493 5.52e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 325 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 404
Cdd:PLN03192  513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 405 SNE---HVLSAG----FEI-------DTPDKFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 470
Cdd:PLN03192  591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                         170       180
                  ....*....|....*....|....*.
gi 1333587291 471 CIETLVTTGANV---NETDDWGRTAL 493
Cdd:PLN03192  670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 22-160 8.49e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  22 EEIRMLIHKTEDVNALDSEKRTPLHVAAflgDAEIIELLILsgarvnakdNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:PTZ00322   42 EEIARIDTHLEALEATENKDATPDHNLT---TEEVIDPVVA---------HMLTVELCQLAASGDAVGARILLTGGADPN 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587291 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:PTZ00322  110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
824-877 8.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 8.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 824 TPLHCAIINDHENCASLLLGAidSSIVNCRDDKGRTPLHAAAFADHVECLQLLL 877
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 209-368 1.02e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHlACYNGQDAVVNE---LTDYGANVN-QPNNSGFTPLHFAAASTH 284
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859  100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                  ....*....
gi 1333587291 360 TSGADTAKC 368
Cdd:PHA02859  180 SLGIDINET 188
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 587-831 1.14e-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: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 654 TPLHASVINGHTLCLRLLLEIADNPEV----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 723 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQIALSEEDCSFKDNQGYTPLHWACYNGN 802
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                         250       260       270
                  ....*....|....*....|....*....|
gi 1333587291 803 ENCIEVLLEQKCF-REFIGNPFTPLHCAII 831
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 587-813 1.48e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASIFVKDNVTKRTPLHASVINghT 665
Cdd:PHA02878   72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--A 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 666 LCLRLLLEIADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEV 745
Cdd:PHA02878  148 EITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 746 SILCKDSRGRTPLHYAAARGHATwlsELLQIALSEEDCSFKDN--QGYTPLHWACYngNENCIEVLLEQK 813
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--SERKLKLLLEYG 290
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291  10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 20-295 2.54e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.21  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946  131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 175 RALH--WAAYMGHLDVVALLIThGAEVTCKDKKGYTPLHAAASNGQinvVKHLLNLGVEIDeiNVYGNTALHLACYNGQD 252
Cdd:PHA02946  210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLS---PAHLINKLLSTS--NVITDQTVNICIFYDRD 283

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1333587291 253 AVVNELTDYGANVNQPNnsgftplhFAAASTHGAL-CLELLVNN 295
Cdd:PHA02946  284 DVLEIINDKGKQYDSTD--------FKMAVEVGSIrCVKYLLDN 319
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-528 2.69e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 471
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 472 ----------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHENSEELERARELKE 526
Cdd:PLN03192  622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQK 701


                  ..
gi 1333587291 527 KE 528
Cdd:PLN03192  702 RE 703
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-493 2.84e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 2.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 364 DTAKCGVHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNV--ECIKL 441
Cdd:PHA02716  275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 442 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA02716  338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 3.05e-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: 44.50  E-value: 3.05e-06
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 3.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333587291 239 GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 781-935 3.31e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 781 EDCSFKDNqgYTPLHWACYNGNENCIEVLLEQKCF-REFIGNPFTPLH-----CAIINDHENCASLLL--GAIdssiVNC 852
Cdd:PHA03100   28 NDYSYKKP--VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGAN----VNA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 853 RDDKGRTPLHAAAFA--DHVECLQLLLRHNAQVNAADNSGKTALMMAAENG-----------QAGA-------VDILVNS 912
Cdd:PHA03100  102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilklliDKGVdinaknrVNYLLSY 181

                         170       180
                  ....*....|....*....|...
gi 1333587291 913 AqADLTVKDKDLNTPLHLASSKP 935
Cdd:PHA03100  182 G-VPINIKDVYGFTPLHYAVYNN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 3.86e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 431-500 4.31e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.31e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 431 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASD 500
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 738-900 5.01e-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: 50.46  E-value: 5.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQialseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 814 CFREFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1333587291 868 DHVECLQLLLRHNAQVNAADNSGKTALMMAAEN 900
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-810 5.39e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 754 GRTPLHYAAARGHatwlSELLQIAL-SEEDCSFKDNQGYTPLHWACYNGNENCIEVLL 810
Cdd:pfam13637   1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-442 7.61e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 7.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 375 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLL 442
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 7.91e-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: 7.91e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1333587291 140 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 171
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 8.39e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.39e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1333587291 618 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 672
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 9.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 669-818 1.30e-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: 48.99  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 669 RLLLEIADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDA---------VDIMGC-----TALH 726
Cdd:cd22194   114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeTPLA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 727 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELL-QIALSEEDCSF---KDNQGYTPLHW 796
Cdd:cd22194   194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273

                         170       180
                  ....*....|....*....|..
gi 1333587291 797 ACYNGNENCIEVLLEqkcfREF 818
Cdd:cd22194   274 AAKMGKAEILKYILS----REI 291
PHA02798 PHA02798
ankyrin-like protein; Provisional
 631-900 1.42e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 631 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDA---VS 705
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 706 LLLEKEANVDAVDIMGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqialseed 782
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 783 csfkdnQGYTPLHwaCY-NGNENCIEV-LLEQKCFREFIGNPFTPLH--------CAIINDHENCASLLLGAIDSSI-VN 851
Cdd:PHA02798  181 ------EKYDTLH--CYfKYNIDRIDAdILKLFVDNGFIINKENKSHkkkfmeylNSLLYDNKRFKKNILDFIFSYIdIN 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1333587291 852 CRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAEN 900
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 735-897 1.70e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 735 ECVQMLLEQEVSILCKD-SRGRTPLHYAAARGHaTWLSELLQIALSEEDCSFKDNQgyTPLHWACYNGNENCIEVLLEQK 813
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKD-QRLTELLLSYGANVNIPDKTNN--SPLHHAVKHYNKPIVHILLENG 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 814 CF---REFIGNpfTPLHCAI--INDHENCASLLLGAIDssiVNCRDD-KGRTPLHAAAFADHVecLQLLLRHNAQVNAAD 887
Cdd:PHA02878  225 AStdaRDKCGN--TPLHISVgyCKDYDILKLLLEHGVD---VNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLN 297

                         170
                  ....*....|
gi 1333587291 888 NSGKTALMMA 897
Cdd:PHA02878  298 SYKLTPLSSA 307
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 1.82e-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: 1.82e-05
                          10        20
                  ....*....|....*....|....*....
gi 1333587291 140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
550-605 2.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 550 GYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLL 605
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 2.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291  93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 561-800 2.39e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.95  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 561 GHRQCLELLLerTNSGFEDSDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 626
Cdd:cd21882     6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 627 FKGHTECVEALINQGASIFVKDNVT--KRTPlhasvingHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAV 704
Cdd:cd21882    82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 705 SLLLE---KEANVDAVDIMGCTALHRGIMTGHEE------CVQM--LLEQEVSILC--------KDSRGRTPLHYAAARG 765
Cdd:cd21882   136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynLLLSYGAHLDptqqleeiPNHQGLTPLKLAAVEG 215

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1333587291 766 HATWLSELLQIALSE--EDCSFKDNQ-GYTPLHWACYN 800
Cdd:cd21882   216 KIVMFQHILQREFSGpyQPLSRKFTEwTYGPVTSSLYD 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 2.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1333587291 132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
790-842 2.52e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.52e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 790 GYTPLHWACYNGNENCIEVLLEQK-CFREFIGNPFTPLHCAIINDHENCASLLL 842
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-81 2.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291  29 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 662-741 2.77e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 662 NGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 741
Cdd:PTZ00322   92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-708 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 1333587291 653 RTPLHASVINGHTLCLRLLLEiadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 708
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 3.92e-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: 47.49  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLITHGAEVTC---- 201
Cdd:cd22196    47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALHL---ACYNGQD------AVVNELT 259
Cdd:cd22196   127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHAlveVADNTPEntkfvtKMYNEIL 206

                         170       180       190
                  ....*....|....*....|....*....|
gi 1333587291 260 DYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd22196   207 ILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
441-496 3.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 441 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 496
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
875-931 4.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587291 875 LLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 856-888 4.37e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 4.37e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1333587291 856 KGRTPLHAAA-FADHVECLQLLLRHNAQVNAADN 888
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
844-897 4.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 844 AIDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMA 897
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 525-711 4.71e-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: 47.31  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 525 KEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLErtnsgfED---------SDSGATKSPLHLAAYN 595
Cdd:cd22192    26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME------AApelvnepmtSDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 596 GHHQALEVLLQSLVDLD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVI 661
Cdd:cd22192   100 QNLNLVRELIARGADVVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVL 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587291 662 NGHTL--C----LRLLLEIADNPEVVD-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 711
Cdd:cd22192   179 QPNKTfaCqmydLILSYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 338-498 4.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 4.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 338 DGNTPLHVAARYGHELLINTLITSGA--DTAKCGVHSmfPLHLAALNAHSDCCRKLLSSGQkysivslfsnehvlsagFE 415
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGK-----------------FA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 416 IDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHY 495
Cdd:PHA02875   95 DDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174


                  ...
gi 1333587291 496 AAA 498
Cdd:PHA02875  175 AMA 177
PHA02791 PHA02791
ankyrin-like protein; Provisional
 768-880 5.29e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.19  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 768 TWLSELLQIALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFREFIGNPFtPLH-CAIINDHENCASLLLGAID 846
Cdd:PHA02791    8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1333587291 847 SSIVncrDDKGRTPLHAAAFADHVECLQLLLRHN 880
Cdd:PHA02791   87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKN 117
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 5.70e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLITHGAE-VTCKDK 204
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEInvygntalHLACYNgqdavvneltdygANVNQ-PNNSGFTPLHF 278
Cdd:cd22194   221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMI--------LLKSEN-------------KNLETiRNNEGLTPLQL 273


                  ..
gi 1333587291 279 AA 280
Cdd:cd22194   274 AA 275
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 7.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 7.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 258 LTDYGANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-399 7.22e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALN 382
Cdd:PTZ00322   79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                          90
                  ....*....|....*..
gi 1333587291 383 AHSDCCRKLLSSGQKYS 399
Cdd:PTZ00322  159 GFREVVQLLSRHSQCHF 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-314 9.99e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1333587291 291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322  166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-708 1.48e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 624 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDvKDakGQTPLMLAVAYGHIDA 703
Cdd:PTZ00322   89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                  ....*
gi 1333587291 704 VSLLL 708
Cdd:PTZ00322  164 VQLLS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 376-494 1.67e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 376 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdkfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 450
Cdd:cd21882    30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 451 ------KKDKC-----GRTPLHYAAANCHFHCIETLVTTG---ANVNETDDWGRTALH 494
Cdd:cd21882   103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 205-234 1.67e-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: 1.67e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
674-726 1.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 674 IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 726
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 2.08e-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: 2.08e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1333587291 272 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-570 2.11e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1333587291 532 CLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLL 570
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-313 2.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 236 NVYGNTALHLACYNGQDAVVNeLTDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884   68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-718 2.53e-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: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1333587291 687 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 718
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 2.65e-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: 39.11  E-value: 2.65e-04
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 2.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1333587291 339 GNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLL 392
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 792-930 2.99e-04

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: 44.62  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 792 TPLHWACYNGNENCIEVLLEQK----CFREFIGNpfTPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTPLHA 863
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 864 AAFADHVECLQLLLRHNAQVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH 174


                  .
gi 1333587291 930 L 930
Cdd:cd22192   175 I 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
587-625 3.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1333587291 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1333587291 236 NVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFA 279
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 213-350 3.82e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVN--------QP--NNSGF----TPLHF 278
Cdd:cd22194   120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194   195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                  ....*.
gi 1333587291 345 VAARYG 350
Cdd:cd22194   273 LAAKMG 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 456-487 5.09e-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: 5.09e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1333587291 456 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 487
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 161-347 5.30e-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: 43.92  E-value: 5.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 161 AKGANINAFDKKDRRALHWAAYMG-HLDVVALLITHGAEVtckdKKGYTPLHAAaSNGQINVVKHLLNLGVEIDEinvyG 239
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAI-SLEYVDAVEAILLHLLAAFR----K 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 240 NTALHLAcyNGQDavvneLTDYGAnvnqpnnsGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVH 316
Cdd:TIGR00870 111 SGPLELA--NDQY-----TSEFTP--------GITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYH 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1333587291 317 GRFTRS-----------QTLIQNGGEIDCVDKDGNTPLHVAA 347
Cdd:TIGR00870 175 GESPLNaaaclgspsivALLSEDPADILTADSLGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 456-484 5.32e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 5.32e-04
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  456 GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 5.53e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 862-931 5.95e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 5.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 862 HAAAFADHVEcLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLA 931
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELA 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
706-761 5.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 706 LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
415-463 6.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 6.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1333587291 415 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 7.92e-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: 7.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1333587291 238 YGNTALHLACY-NGQDAVVNELTDYGANVNQPNN 270
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 8.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333587291  65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 205-234 8.22e-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: 8.22e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1333587291 205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 693-785 8.22e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 693 MLAVAYGHIDA------VSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 764
Cdd:PTZ00322   81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158

                          90       100
                  ....*....|....*....|.
gi 1333587291 765 GhatwLSELLQIALSEEDCSF 785
Cdd:PTZ00322  159 G----FREVVQLLSRHSQCHF 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 856-885 8.28e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.57  E-value: 8.28e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  856 KGRTPLHAAAFADHVECLQLLLRHNAQVNA 885
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 423-572 8.75e-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: 43.21  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 423 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVTTGA-NVNETDD 487
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 488 WGRTALH--YAAASDMDRNKTILGNAHEnseELERARELKEKEAasclefllqneanpsIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22194   221 RGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------IRNNEGLTPLQLAAKMGKAEI 282


                  ....*..
gi 1333587291 566 LELLLER 572
Cdd:cd22194   283 LKYILSR 289
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 423-576 9.52e-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: 42.92  E-value: 9.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 423 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 486
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 487 DWGRTALHYAAasdmdrnkTILGNAHENSEELERA-RELKEKEAASCLEFLLQneanpSIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22197   174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240

                         170
                  ....*....|.
gi 1333587291 566 LELLLERTNSG 576
Cdd:cd22197   241 FRHILQREFSG 251
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 586-637 1.00e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 586 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 637
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 409-466 1.04e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 409 VLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 466
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 40-180 1.15e-03

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: 42.56  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 104 DKNWQTPLH--VAAANKAVKCAEVII--------------PLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANiN 167
Cdd:cd21882   152 DSLGNTVLHalVLQADNTPENSAFVCqmynlllsygahldPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS-G 230

                         170
                  ....*....|...
gi 1333587291 168 AFDKKDRRALHWA 180
Cdd:cd21882   231 PYQPLSRKFTEWT 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 1.22e-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: 1.22e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1333587291  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 1.32e-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: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallithgaevtckdkkgytPLHAA 213
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHLACYNGQDAVVN---------ELTDYGANVNQ-------PNNSGFT 274
Cdd:cd22197   148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                  ....*.
gi 1333587291 275 PLHFAA 280
Cdd:cd22197   228 PLKLAA 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-318 1.36e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 189 VALLITHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhlacyngqDAV-VNELTDYGANVN 266
Cdd:PTZ00322   44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 267 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322  110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 789-811 1.44e-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: 36.80  E-value: 1.44e-03
                           10        20
                   ....*....|....*....|...
gi 1333587291  789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-716 1.44e-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: 36.85  E-value: 1.44e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1333587291 687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 647-759 1.51e-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: 42.48  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 647 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 714
Cdd:cd22193    24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333587291 715 DAVD--------------IMGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 759
Cdd:cd22193   103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
PHA02795 PHA02795
ankyrin-like protein; Provisional
 124-201 1.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.90  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLITH 195
Cdd:PHA02795  205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                  ....*.
gi 1333587291 196 GAEVTC 201
Cdd:PHA02795  285 PLSIDC 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-364 1.89e-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: 1.89e-03
                           10        20
                   ....*....|....*....|....*..
gi 1333587291  338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 617-649 1.92e-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: 1.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1333587291 617 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 649
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 423-451 1.93e-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: 1.93e-03
                           10        20
                   ....*....|....*....|....*....
gi 1333587291  423 GRTCLHAAAAGGNVECIKLLQSSGADFHK 451
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 43-121 2.29e-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: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          90
                  ....*....|...
gi 1333587291 109 TPLHVAAANKAVK 121
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 687-716 2.37e-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: 2.37e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 140-282 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLITHG---AEVTCK 202
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHLACYNGqdavvneLTDYGANVNQP-------NNSGFTP 275
Cdd:cd22193   156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                  ....*..
gi 1333587291 276 LHFAAAS 282
Cdd:cd22193   212 LQLAAKM 218
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 829-932 2.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 829 AIINDHENCASLLLgaiDSSI-VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:PHA02875    9 AILFGELDIARRLL---DIGInPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                          90       100
                  ....*....|....*....|....*
gi 1333587291 908 ILVNSAQADLTVKDKDLNTPLHLAS 932
Cdd:PHA02875   86 ELLDLGKFADDVFYKDGMTPLHLAT 110
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-204 2.99e-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: 2.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1333587291 176 ALHWAAYM-GHLDVVALLITHGAEVTCKDK 204
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 690-862 3.27e-03

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: 41.15  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 690 TPLMLAVAYGHIDAVS-LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEqevsilckdsrgrtplhyaAARGhat 768
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-------------------AAPE--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 769 wlsellqiaLSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQ-----------KCFREFIGNPFT----PLHCAIIND 833
Cdd:cd22192    77 ---------LVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVG 147

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1333587291 834 HENCASLLL--GAidsSIVNcRDDKGRTPLH 862
Cdd:cd22192   148 NEEIVRLLIehGA---DIRA-QDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 3.31e-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: 41.22  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgvhsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870 116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                         170       180
                  ....*....|....*....|....*
gi 1333587291 470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH 213
PHA02791 PHA02791
ankyrin-like protein; Provisional
 40-237 3.62e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 119
Cdd:PHA02791   60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 120 vkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLITHGAE 198
Cdd:PHA02791  124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1333587291 199 VTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02791  186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 55-195 4.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291  55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884   47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLITH 195
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 4.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587291 291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
 144-275 5.33e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791   65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587291 223 KHLLNlgveidEINVYGNTALHLACY-----NGQDAVVNELTDYGANVNQPNNSGFTP 275
Cdd:PHA02791  145 SYFLS------EIPSTFDLAILLSCIhitikNGHVDMMILLLDYMTSTNTNNSLLFIP 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 617-646 5.75e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 5.75e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587291  617 KGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
745-797 5.88e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 745 VSILCKDSRGRTPLHYAAARGHATWLSELLqiaLSEEDCSFKDNQGYTPLHWA 797
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 423-454 5.96e-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: 5.96e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1333587291 423 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 454
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 6.14e-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: 35.34  E-value: 6.14e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1333587291  76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 455-484 6.29e-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: 6.29e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1333587291 455 CGRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-201 6.47e-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: 34.87  E-value: 6.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 1333587291  176 ALHWAAYMGHLDVVALLITHGAEVTC 201
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 7.15e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.15e-03
                          10        20
                  ....*....|....*....|....*....
gi 1333587291 238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 214-496 7.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.11  E-value: 7.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HLACYNGQDAVVNELTDYGANVNQpnnSGF--TPL-----HFAAAST 283
Cdd:PHA02989   11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989   86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587291 354 LINT-----LITSGADTakcgVHSMFPLHLAALNAHSDccrkllssgQKYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLH 428
Cdd:PHA02989  157 SVKKdvikiLLSFGVNL----FEKTSLYGLTPMNIYLR---------NDIDVISIKVIKYLIKKGVNIETNNNGSESVLE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587291 429 AAAAGGNV---ECIKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 496
Cdd:PHA02989  224 SFLDNNKIlskKEFKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH