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Conserved domains on  [gi|62988328|ref|NP_065070|]
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ankyrin repeat domain-containing protein 50 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
558-851 7.11e-62

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.66  E-value: 7.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666  161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62988328  798 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
833-1102 4.60e-59

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250       260       270
                 ....*....|....*....|....*....|
gi 62988328 1073 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
495-609 1.70e-13

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100  157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62988328   575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Semenogelin super family cl28737
Semenogelin; This family consists of several mammalian secreted seminal proteins including ...
1210-1403 7.03e-07

Semenogelin; This family consists of several mammalian secreted seminal proteins including semenogelin I and II. Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle secreted semenogelins (Sg). This family also includes seminal vesicle secretory protein 3A from mouse, which has been shown to be involved in the coagulation of semen resulting in the formation of the copulatory plug.


The actual alignment was detected with superfamily member pfam05474:

Pssm-ID: 368458 [Multi-domain]  Cd Length: 582  Bit Score: 53.73  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   1361 --------------IMTNPNYHLQSNQvflgRVSVPRTMQDRGHQEVLEGYPSSETE 1403
Cdd:pfam05474  422 ekdvqkgvskgsisIQTEEKIHGKSQN----QVTIPSQDQEHGHKENKMSYQSSSTE 474
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
22-195 1.65e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


:

Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.95  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328     22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 62988328    175 LPllgmKPPQQSLYLLVDSVD 195
Cdd:pfam13191  126 LL----ARGERPLVLVLDDLQ 142
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
558-851 7.11e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.66  E-value: 7.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666  161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62988328  798 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
833-1102 4.60e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250       260       270
                 ....*....|....*....|....*....|
gi 62988328 1073 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
625-907 1.27e-36

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 145.55  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA03095  183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   853 MAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA03095  263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA02876 PHA02876
ankyrin repeat protein; Provisional
763-1102 1.07e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.94  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876  240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   922 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PHA02876  316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   995 VQVLIAYHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 1072
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|
gi 62988328  1073 HADQFGRTAMRVAAknGHSQIIKLLEKYGA 1102
Cdd:PHA02876  471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
983-1075 9.49e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 9.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    983 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 1062
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328   1063 VLLEHGADPNHAD 1075
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
752-844 5.04e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 5.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 62988328    831 RTLLDRGLDENHRD 844
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
495-609 1.70e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100  157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62988328   575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
864-1093 4.80e-12

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 70.43  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 942
Cdd:cd22192    7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 1015
Cdd:cd22192   71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 1067
Cdd:cd22192  129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
                        250       260
                 ....*....|....*....|....*.
gi 62988328 1068 gaDPNHAdqfGRTAMRVAAKNGHSQI 1093
Cdd:cd22192  207 --VPNNQ---GLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
580-761 1.40e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192   91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328  706 EDVDGRTALSVAALcvPASKGHASVVSLLI------DRGAEVDHC-DKDGMTPLLVAAYEGHV 761
Cdd:cd22192  165 QDSLGNTVLHILVL--QPNKTFACQMYDLIlsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNI 225
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
807-964 1.57e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.24  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870  121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
                          170       180
                   ....*....|....*....|....*.
gi 62988328    939 VNCKDADGRPTLYILALENQLTmAEY 964
Cdd:TIGR00870  201 ILTADSLGNTLLHLLVMENEFK-AEY 225
Semenogelin pfam05474
Semenogelin; This family consists of several mammalian secreted seminal proteins including ...
1210-1403 7.03e-07

Semenogelin; This family consists of several mammalian secreted seminal proteins including semenogelin I and II. Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle secreted semenogelins (Sg). This family also includes seminal vesicle secretory protein 3A from mouse, which has been shown to be involved in the coagulation of semen resulting in the formation of the copulatory plug.


Pssm-ID: 368458 [Multi-domain]  Cd Length: 582  Bit Score: 53.73  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   1361 --------------IMTNPNYHLQSNQvflgRVSVPRTMQDRGHQEVLEGYPSSETE 1403
Cdd:pfam05474  422 ekdvqkgvskgsisIQTEEKIHGKSQN----QVTIPSQDQEHGHKENKMSYQSSSTE 474
Ank_4 pfam13637
Ankyrin repeats (many copies);
513-565 1.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    513 RTSCIVRQA-LEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLV 565
Cdd:pfam13637    1 ELTALHAAAaSGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1044-1072 2.93e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.93e-05
                            10        20
                    ....*....|....*....|....*....
gi 62988328    1044 QGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
747-775 6.11e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 6.11e-05
                            10        20
                    ....*....|....*....|....*....
gi 62988328     747 DGMTPLLVAAYEGHVDVVDLLLEGGADVD 775
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
22-195 1.65e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.95  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328     22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 62988328    175 LPllgmKPPQQSLYLLVDSVD 195
Cdd:pfam13191  126 LL----ARGERPLVLVLDDLQ 142
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
558-851 7.11e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.66  E-value: 7.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666  161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62988328  798 NTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
629-917 9.03e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.50  E-value: 9.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  629 ALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDV 708
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  709 DGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:COG0666   86 GGNTLLHAAA-----RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIE 868
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62988328  869 QGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNAL 917
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
833-1102 4.60e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.57  E-value: 4.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250       260       270
                 ....*....|....*....|....*....|
gi 62988328 1073 HADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
531-818 5.45e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.49  E-value: 5.45e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  531 LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR 690
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  691 EIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEG 770
Cdd:COG0666  167 EIVKLLLEAGADVNARDNDGETPLHLA-----AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 62988328  771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVL 818
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
861-1102 1.63e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 198.25  E-value: 1.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  861 LICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVN 940
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  941 CKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAA 1020
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1021 WQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKY 1100
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                 ..
gi 62988328 1101 GA 1102
Cdd:COG0666  242 GA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
728-1016 1.13e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.86  E-value: 1.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  728 ASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAV 807
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  808 DSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  888 SQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLE 967
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62988328  968 NGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSAL 1016
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
495-752 2.57e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 191.71  E-value: 2.57e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  495 EVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:COG0666   37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWG 654
Cdd:COG0666  117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  655 GHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLL 734
Cdd:COG0666  197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA-----AGAALIVKLL 271
                        250
                 ....*....|....*...
gi 62988328  735 IDRGAEVDHCDKDGMTPL 752
Cdd:COG0666  272 LLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
707-983 7.61e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 190.55  E-value: 7.61e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  707 DVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLL 786
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  787 AAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  867 IEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADG 946
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 62988328  947 RPTLYILALENQLTMAEYFLENGANVEASDAEGRTAL 983
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
804-1082 1.60e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.39  E-value: 1.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:COG0666   11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  884 FILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCN 1043
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 62988328 1044 QGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAM 1082
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
761-1049 1.32e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 186.70  E-value: 1.32e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  761 VDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  841 NHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  921 ALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA 1000
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62988328 1001 YHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATAL 1049
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
443-714 8.95e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.61  E-value: 8.95e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  443 QAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQAL 522
Cdd:COG0666   16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  523 E--REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:COG0666   96 RngDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  601 GANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTA 680
Cdd:COG0666  176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
                        250       260       270
                 ....*....|....*....|....*....|....
gi 62988328  681 LIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:COG0666  256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
625-907 1.27e-36

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 145.55  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA03095  183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   853 MAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA03095  263 YAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
524-836 2.68e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 132.46  E-value: 2.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   524 REDSIRTLLDNGASVNQCDSNGRTLLA---NAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT-KVVNCLIG 599
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   600 CGANINHTDQDGWTALrsaawggHTevvsallYAGVKvdcadadsRTalraaawggHEDIVLNLLQHGAEVNKADNEGRT 679
Cdd:PHA03095  106 AGADVNAKDKVGRTPL-------HV-------YLSGF--------NI---------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   680 ALiaAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:PHA03095  155 PL--AVLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   756 AYEGHVD--VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTL 833
Cdd:PHA03095  230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                  ...
gi 62988328   834 LDR 836
Cdd:PHA03095  310 LAK 312
PHA02876 PHA02876
ankyrin repeat protein; Provisional
558-900 1.16e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 133.65  E-value: 1.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   638 DCADADSRTALRaaawggHEDIVLNLLQH--GAEVNKADNEGRTALIAAAYMGH-REIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:PHA02876  238 NKNDLSLLKAIR------NEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   715 SVAalcvpASKGHASV-VSLLIDRGAEVDHCDKDGMTPLLVAA-YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 792
Cdd:PHA02876  312 YLM-----AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   793 HASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEV-VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQG 870
Cdd:PHA02876  387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNG 466
                         330       340       350
                  ....*....|....*....|....*....|
gi 62988328   871 ARTNEIDNDGRIPFILASqeGHYDCVQILL 900
Cdd:PHA02876  467 ADVNAINIQNQYPLLIAL--EYHGIVNILL 494
PHA02874 PHA02874
ankyrin repeat protein; Provisional
686-1014 1.35e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 123.92  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   686 YMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PHA02874   10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAI----RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   766 LLLEGGADvdhtdnngrTPLLAAASMgHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDD 845
Cdd:PHA02874   86 LLIDNGVD---------TSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   846 AGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEgH 925
Cdd:PHA02874  156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-N 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   926 RDIVELLFSHgADVNCKDADG-RPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSC-WQGHMEMVQVLIAYHA 1003
Cdd:PHA02874  235 RSAIELLINN-ASINDQDIDGsTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAV 313
                         330
                  ....*....|.
gi 62988328  1004 DVNAADNEKRS 1014
Cdd:PHA02874  314 LIKEADKLKDS 324
PHA02876 PHA02876
ankyrin repeat protein; Provisional
763-1102 1.07e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.94  E-value: 1.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876  240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   922 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PHA02876  316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   995 VQVLIAYHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 1072
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|
gi 62988328  1073 HADQFGRTAMRVAAknGHSQIIKLLEKYGA 1102
Cdd:PHA02876  471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
480-717 1.50e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.20  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSeddRTSC-------IVRQAlEREDSIRTLLDNGASVNQCDSNGRTLLAna 552
Cdd:PHA03095   49 TPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCgftplhlYLYNA-TTLDVIKLLIKAGADVNAKDKVGRTPLH-- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   553 AYSGSL----DVVNLLVSRGADLEIEDAHGHTPLT--LAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHT-- 624
Cdd:PHA03095  123 VYLSGFninpKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHED--IVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282
                         250
                  ....*....|....*
gi 62988328   703 VNHEDVDGRTALSVA 717
Cdd:PHA03095  283 INAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
557-851 3.22e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 117.05  E-value: 3.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   557 SLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGH---TKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTE-VVSALLY 632
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   633 AGVKVDCADADSRTALRAAAWGG--HEDIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR----EIVEHLLDHGAEVNHE 706
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRnanvELLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   707 DVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA03095  184 DDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTP 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   785 LLAAAsmghasvvntllfwgaavdsidsegrtvlsiasAQGNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:PHA03095  261 LHYAA---------------------------------VFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
862-1103 7.06e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 112.45  E-value: 7.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   862 ICEALIEQGARTNEIDNDGRIPFILASQEGHydcvqillenksnidqrgydgrNALRVaaleghRDIVELLFSHGADVNC 941
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKY----------------------NLTDV------KEIVKLLLEYGANVNA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   942 KDADGRPTLYILALE--NQLTMAEYFLENGANVEASDAEGRTALH--VSCWQGHMEMVQVLIAYHADVNAADNekrsalq 1017
Cdd:PHA03100  102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLLIDKGVDINAKNR------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1018 saawqghvkvVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA03100  175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                  ....*.
gi 62988328  1098 EKYGAS 1103
Cdd:PHA03100  245 LNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
658-983 1.04e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.73  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   658 DIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSvaalCVPASKGHASVVS 732
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPL--HLYLHYSsekvkDIVRLLLEAGADVNAPERCGFTPLH----LYLYNATTLDVIK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   733 LLIDRGAEVDHCDKDGMTPLLV--AAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASV--VNTLLFWGAAVD 808
Cdd:PHA03095  102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   809 SIDSEGRTVLSI--ASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHrliCEALIEQgartneidndgriPFIL 886
Cdd:PHA03095  182 AVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVL-------------PLLI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   887 AsqeghydcvqillenksnidqrgydgrnalrvaaleghrdivellfshGADVNCKDADGRPTLYILALENQLTMAEYFL 966
Cdd:PHA03095  246 A------------------------------------------------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277
                         330
                  ....*....|....*..
gi 62988328   967 ENGANVEASDAEGRTAL 983
Cdd:PHA03095  278 ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
820-1095 1.93e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 1.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   820 IASAQGNVEVVRTLLDRGLDENHRDDAGWTPLH--MAAFEGHRL-ICEALIEQGARTNEIDNDGRIPFIL----ASQEgh 892
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLylynATTL-- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   893 yDCVQILLENKSNIDQRGYDGRNALRV--AALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMA--EYFLEN 968
Cdd:PHA03095   98 -DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   969 GANVEASDAEGRTALHVscwqgHME-------MVQVLIAYHADVNAADNEKRSALQSAAWQGHVK--VVQLLIEHGAVVD 1039
Cdd:PHA03095  177 GADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328  1040 HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIK 1095
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
625-842 2.66e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.44  E-value: 2.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE-----DIVLNLLQHGAEVNKADNEGRTALIAAAY--MGHREIVEHLL 697
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   698 DHGAEVNHEDVDGRTALSVAALCVPASKghaSVVSLLIDRGAEVDHCDKdgmtpllvaayeghvdvVDLLLEGGADVDHT 777
Cdd:PHA03100  129 DNGANVNIKNSDGENLLHLYLESNKIDL---KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   778 DNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
606-797 1.74e-23

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 108.03  E-value: 1.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   606 HTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAA 685
Cdd:PLN03192  520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   686 YMGHREIVeHLLDHGAEVNHEDVDGRTalsvaaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PLN03192  600 SAKHHKIF-RILYHFASISDPHAAGDL------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 62988328   766 LLLEGGADVDHTD-NNGRTP-----LLAAASMGHASVV 797
Cdd:PLN03192  673 LLIMNGADVDKANtDDDFSPtelreLLQKRELGHSITI 710
PHA02874 PHA02874
ankyrin repeat protein; Provisional
492-788 5.96e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.81  E-value: 5.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   492 KEQEVLQLLVKA-GAHVNSEDDRTSCIVRQALEREDS--IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRG 568
Cdd:PHA02874   12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAkiVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   569 ADLEIedahghtpltLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTAL 648
Cdd:PHA02874   92 VDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   649 RAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaskGHA 728
Cdd:PHA02874  162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII------HNR 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328   729 SVVSLLIDrGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:PHA02874  236 SAIELLIN-NASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
983-1075 9.49e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 9.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    983 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 1062
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328   1063 VLLEHGADPNHAD 1075
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
826-1044 1.75e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.97  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-----ICEALIEQGARTNEIDNDGRIP-FILASQE-GHYDCVQI 898
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPlLYAISKKsNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   899 LLENKSNIDQRGYDGRNALRVAALEGHRD--IVELLFSHGADVNCKDAdgrptlyilalenqltmAEYFLENGANVEASD 976
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328   977 AEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQ 1044
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
851-943 3.23e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 3.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    851 LHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKsNIDQRGYdGRNALRVAALEGHRDIVE 930
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328    931 LLFSHGADVNCKD 943
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
718-940 2.08e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   718 ALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   798 NTLLFWGA-AVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEI 876
Cdd:PHA02875   85 EELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   877 DNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHR-DIVELLFSHGADVN 940
Cdd:PHA02875  165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
761-945 9.13e-20

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 96.09  E-value: 9.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   761 VDVVDLLLEGGADvdHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:PLN03192  507 LNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   841 NHRDDAGWTPLHMAAFEGHRLICEALiEQGARTNEIDNDGRIpFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:PLN03192  585 HIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
                         170       180
                  ....*....|....*....|....*
gi 62988328   921 ALEGHRDIVELLFSHGADVNCKDAD 945
Cdd:PLN03192  663 MAEDHVDMVRLLIMNGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
752-844 5.04e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 5.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 62988328    831 RTLLDRGLDENHRD 844
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
891-1104 5.16e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 91.21  E-value: 5.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   891 GHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEngA 970
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--L 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   971 NVEASDA---EGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02875   91 GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328  1048 ALCIAAQEGHIDVVQVLLEHGADPNHadqFGR----TAMRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADC 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
618-707 5.78e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 5.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    618 AAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHgAEVNKADNeGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
                           90
                   ....*....|
gi 62988328    698 DHGAEVNHED 707
Cdd:pfam12796   82 EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
818-909 6.37e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 6.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    818 LSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARtnEIDNDGRIPFILASQEGHYDCVQ 897
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 62988328    898 ILLENKSNIDQR 909
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
582-674 7.44e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 7.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    582 LTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLyAGVKVDCADaDSRTALRAAAWGGHEDIVL 661
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328    662 NLLQHGAEVNKAD 674
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
824-1121 1.12e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 92.05  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   824 QGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   904 SNIDQRGYDGRNALRVAALEGH------------------------------RDIVELLFSHGADVNCKDADGRPTLYIL 953
Cdd:PHA02876  235 SNINKNDLSLLKAIRNEDLETSlllydagfsvnsiddckntplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   954 A-----LENQLTMaeyfLENGANVEASDAEGRTALH-VSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKV 1027
Cdd:PHA02876  315 AkngydTENIRTL----IMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1028 VQLLIEHGAVVDHTCNQGATALCIA-AQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNG-HSQIIKLLEKygassl 1105
Cdd:PHA02876  391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLD------ 464
                         330
                  ....*....|....*.
gi 62988328  1106 NGCSPSPVHTMEQKPL 1121
Cdd:PHA02876  465 NGADVNAINIQNQYPL 480
PHA03100 PHA03100
ankyrin repeat protein; Provisional
524-746 1.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.49  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   524 REDSIRTLLDNGASVNQCDSNGRTLL---ANAAYSGS--LDVVNLLVSRGADLEIEDAHGHTPLTLAA--RQGHTKVVNC 596
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLhylSNIKYNLTdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   597 LIGCGANINHTDQDGWTALRSAAWGGH--TEVVSALLYAGVKVDCADAdsrtalraaawgghediVLNLLQHGAEVNKAD 674
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   675 NEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL-----NNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
724-1087 1.33e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.41  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   724 SKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   804 GaaVDSidsegrTVLSIASAqgNVEVVRTLLDRGLDENHRDDAGWTPLHMAafeghrlicealieqgartneIDNdgrip 883
Cdd:PHA02874   91 G--VDT------SILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYA---------------------IKK----- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   884 filasqeghydcvqillenksnidqrgydgrnalrvaaleGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:PHA02874  135 ----------------------------------------GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHvKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID 253
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 62988328  1044 qGATALCIAAQ-EGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874  254 -GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
959-1102 1.49e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVV 1038
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328 1039 DHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
723-811 3.60e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    723 ASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEgGADVDHTDnNGRTPLLAAASMGHASVVNTLLF 802
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82

                   ....*....
gi 62988328    803 WGAAVDSID 811
Cdd:pfam12796   83 KGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
648-742 4.59e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 4.59e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    648 LRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHgAEVNHEDvDGRTALSVAalcvpASKGH 727
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA-----ARSGH 73
                           90
                   ....*....|....*
gi 62988328    728 ASVVSLLIDRGAEVD 742
Cdd:pfam12796   74 LEIVKLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
549-641 8.40e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 8.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCgANINHTDqDGWTALRSAAWGGHTEVVS 628
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328    629 ALLYAGVKVDCAD 641
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
950-1041 9.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 9.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    950 LYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAyHADVNAADNeKRSALQSAAWQGHVKVVQ 1029
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 62988328   1030 LLIEHGAVVDHT 1041
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
917-1009 1.31e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    917 LRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENgANVEASDaEGRTALHVSCWQGHMEMVQ 996
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 62988328    997 VLIAYHADVNAAD 1009
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
896-1114 1.34e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.77  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   896 VQILLENKSNIDQRGYDGRNALRV---AALEGHRDIVELLFSHGADVNCKDADG-RPTLYILALENQLTMAEYFLENGAN 971
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDVIKLLIKAGAD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   972 VEASDAEGRTALHVsCWQG---HMEMVQVLIAYHADVNAADNEKRSALQ-----SAAwqgHVKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA03095  110 VNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328  1044 QGATALCIAAQEGHID--VVQVLLEHGADPNHADQFGRTAMRVAAKNG---HSQIIKLLEKyGAS--SLNGCSPSPVH 1114
Cdd:PHA03095  186 RFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISinARNRYGQTPLH 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1016-1103 1.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHgADPNHADQfGRTAMRVAAKNGHSQIIK 1095
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                   ....*...
gi 62988328   1096 LLEKYGAS 1103
Cdd:pfam12796   79 LLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
826-1087 2.87e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.47  E-value: 2.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIpfilaSQEGHYDCVQI---LLEN 902
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAI-----KDAFNNRNVEIfkiILTN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   903 KSN---------IDQRGYDGrnalrvaALEGhrDIVELLFSHGADVNCKDADGRPTLYILALENQLT-MAEYFLENGANV 972
Cdd:PHA02878  124 RYKniqtidlvyIDKKSKDD-------IIEA--EITKLLLSYGADINMKDRHKGNTALHYATENKDQrLTELLLSYGANV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   973 EASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAwqGHVK---VVQLLIEHGAVVD-HTCNQGATA 1048
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNaKSYILGLTA 272
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 62988328  1049 LCIAAQEGhiDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02878  273 LHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
963-1119 5.75e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 86.85  E-value: 5.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   963 EYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVD-HT 1041
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA 621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1042 cnqGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS-----SLNGCSPSPVHTM 1116
Cdd:PLN03192  622 ---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkanTDDDFSPTELREL 698

                  ...
gi 62988328  1117 EQK 1119
Cdd:PLN03192  699 LQK 701
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
659-925 1.24e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   659 IVLNLLQHGAEVNKADnegrtaliaaaymghreiVEHLLdhgAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRG 738
Cdd:PLN03192  493 ILKNFLQHHKELHDLN------------------VGDLL---GDNGGEHDDPNMASNLLTV---ASTGNAALLEELLKAK 548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   739 AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSidSEGRTVL 818
Cdd:PLN03192  549 LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLL 626
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   819 SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDND------------------G 880
Cdd:PLN03192  627 CTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfsptelrellqkrelgH 706
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 62988328   881 RIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGH 925
Cdd:PLN03192  707 SITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQCRPRVSIYKGH 751
PHA02875 PHA02875
ankyrin repeat protein; Provisional
544-773 1.39e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.89  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   544 NGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGH 623
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   624 TEVVSALLYAGVKV-DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA02875   81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   703 VNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-VDVVDLLLEGGAD 773
Cdd:PHA02875  161 LDIEDCCGCTPLIIA-----MAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNkIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
645-874 7.78e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.58  E-value: 7.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpas 724
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   725 KGHASVVSLLIDRGAEVDHC-DKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02875   78 EGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQGARTN 874
Cdd:PHA02875  158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCN 229
PHA02798 PHA02798
ankyrin-like protein; Provisional
730-1010 1.36e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 81.42  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   730 VVSLLIDRGAEVDHCDKDGMTPLL-----VAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW- 803
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMi 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   804 --GAAVDSIDSEGRTVLSIASAQGN---VEVVRTLLDRGLDEN-HRDDAGWTPLH-MAAFEGHRL---ICEALIEQGART 873
Cdd:PHA02798  133 enGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHcYFKYNIDRIdadILKLFVDNGFII 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   874 NEIDNDGRIPFIlasqeghyDCVQILLENKSNIDqrgydgrnalrvaaleghRDIVELLFSHgADVNCKDADGRPTLYIL 953
Cdd:PHA02798  213 NKENKSHKKKFM--------EYLNSLLYDNKRFK------------------KNILDFIFSY-IDINQVDELGFNPLYYS 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   954 ALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADN 1010
Cdd:PHA02798  266 VSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISY 322
PHA02878 PHA02878
ankyrin repeat protein; Provisional
549-824 5.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.54  E-value: 5.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAA----RQGHTKVVNCLIGCgaNINHTDQdgwtALRSAAWGGHT 624
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKC--SVFYTLV----AIKDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKAD-NEGRTALIAAAYMGHREIVEHLLDHGAEV 703
Cdd:PHA02878  115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   704 NHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDN-NG 781
Cdd:PHA02878  195 NIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLG 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 62988328   782 RTPLlaAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQ 824
Cdd:PHA02878  270 LTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
526-608 1.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 1.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRgADLEIEDaHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:pfam12796   11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88

                   ...
gi 62988328    606 HTD 608
Cdd:pfam12796   89 VKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
815-1072 2.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   815 RTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYD 894
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   895 CVQILLENKSNIDQRGY-DGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRptlyilalenqltmaeyflenganve 973
Cdd:PHA02875   83 AVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-------------------------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   974 asdaegrTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQG-ATALCIA 1052
Cdd:PHA02875  137 -------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYA 209
                         250       260
                  ....*....|....*....|
gi 62988328  1053 AQEGHIDVVQVLLEHGADPN 1072
Cdd:PHA02875  210 IENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
915-1094 3.86e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.60  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   915 NALRVAALeGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PLN03192  528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   995 VQVLiaYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHA 1074
Cdd:PLN03192  607 FRIL--YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
                         170       180
                  ....*....|....*....|....*.
gi 62988328  1075 ---DQFGRTAMRVAAKN---GHSQII 1094
Cdd:PLN03192  685 ntdDDFSPTELRELLQKrelGHSITI 710
PHA03100 PHA03100
ankyrin repeat protein; Provisional
495-634 5.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 5.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVNSEDDRTSCIVRQALERE----DSIRTLLDNGASVNQCDSNGRTLLANAAYSGS--LDVVNLLVSRG 568
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   569 ADLEIE----------------DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 632
Cdd:PHA03100  167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                  ..
gi 62988328   633 AG 634
Cdd:PHA03100  247 NG 248
PHA02874 PHA02874
ankyrin repeat protein; Provisional
851-1115 1.09e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   851 LHMAAFEGHRLICEALIEQgaRTNEID---NDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRD 927
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKN--KGNCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   928 IVELLFSHGADVNckdadgrpTLYILALENQltMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:PHA02874   83 IIKLLIDNGVDTS--------ILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1008 ADNekrsalqsaawqghvkvvqlliehgavvdhtcnQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874  153 EDD---------------------------------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                         250       260       270
                  ....*....|....*....|....*....|
gi 62988328  1088 NGHSQIIKLLEKYGASSLNGCSP--SPVHT 1115
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCKNgfTPLHN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
495-609 1.70e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100  157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62988328   575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA03100  222 NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
751-1034 5.68e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 5.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   751 PLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA-------------ASMGHASVVNTLLFWGAAVDSIDSEGRTV 817
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   818 LSIASAQGN------------------VEVVRTLLDRGLDENHRD-DAGWTPLHMAAFEGHRLICEALIEQGARTNEIDN 878
Cdd:PHA02878  120 ILTNRYKNIqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   879 DGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNCKDadgrptlYILALen 957
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-------YILGL-- 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328   958 qltmaeyflenganveasdaegrTALHVSCwqgHMEMV-QVLIAYHADVNAADNEKRSALQSAAWQGH-VKVVQLLIEH 1034
Cdd:PHA02878  271 -----------------------TALHSSI---KSERKlKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
526-740 1.26e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   606 HT-DQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAA 684
Cdd:PHA02875   96 DVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328   685 AYMGHREIVEHLLDHGAEVNHEDVDGrtalSVAALCVPASKGHASVVSLLIDRGAE 740
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNG----CVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
748-801 3.45e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 3.45e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    748 GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
495-631 3.57e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGS---LDVVNLLVsR 567
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLLI-A 246
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328   568 GADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 631
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
864-1093 4.80e-12

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 70.43  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 942
Cdd:cd22192    7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 1015
Cdd:cd22192   71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 1067
Cdd:cd22192  129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
                        250       260
                 ....*....|....*....|....*.
gi 62988328 1068 gaDPNHAdqfGRTAMRVAAKNGHSQI 1093
Cdd:cd22192  207 --VPNNQ---GLTPFKLAAKEGNIVM 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
1047-1097 1.94e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.94e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 62988328   1047 TALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
497-649 2.87e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   497 LQLLVKAG--AHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGAdleIE 574
Cdd:PLN03192  541 LEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328   575 DAH-GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADAD---SRTALR 649
Cdd:PLN03192  618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELR 696
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
706-801 4.75e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 4.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   706 EDVDGRTA--LSVAaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRT 783
Cdd:PTZ00322   72 EVIDPVVAhmLTVE-LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
                          90
                  ....*....|....*...
gi 62988328   784 PLLAAASMGHASVVNTLL 801
Cdd:PTZ00322  151 PLELAEENGFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
759-987 8.56e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 8.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   759 GHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGl 838
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   839 deNHRDDA----GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGR 914
Cdd:PHA02875   92 --KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   915 NALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAEYFLENGAN---VEASDAEGRTALHVSC 987
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIEnNKIDIVRLFIKRGADcniMFMIEGEECTILDMIC 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
764-850 1.13e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.07  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   764 VDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRtLLDRGLDENHR 843
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176

                  ....*..
gi 62988328   844 DDAGWTP 850
Cdd:PTZ00322  177 LGANAKP 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1028-1130 1.48e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1028 VQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNG 1107
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
                          90       100
                  ....*....|....*....|...
gi 62988328  1108 CSPSPVHTMEQKPLQSLSSKVQS 1130
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLEDSPISS 200
Ank_4 pfam13637
Ankyrin repeats (many copies);
814-867 4.95e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 4.95e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    814 GRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALI 867
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
528-719 7.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   528 IRTLLDNGASVNQCDSN-GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:PHA02878  150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   607 TDQDGWTALrsaawggHTEVVSALLYagvkvdcadadsrtalraaawggheDIVLNLLQHGAEVN-KADNEGRTALIAAa 685
Cdd:PHA02878  230 RDKCGNTPL-------HISVGYCKDY-------------------------DILKLLLEHGVDVNaKSYILGLTALHSS- 276
                         170       180       190
                  ....*....|....*....|....*....|....
gi 62988328   686 yMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAL 719
Cdd:PHA02878  277 -IKSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
889-1114 8.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 8.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   889 QEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEN 968
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   969 GANVEASDAEGRTALHvscwqgHMEMVQVLIAYHA--DVNAADNEKRSALQSAAWQGHV-KVVQLLIEHGAVVDHTCNQG 1045
Cdd:PHA02876  234 RSNINKNDLSLLKAIR------NEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKG 307
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62988328  1046 ATALCIAAQEGH-IDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQ--IIKLLEkYGA--SSLNGCSPSPVH 1114
Cdd:PHA02876  308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdiVITLLE-LGAnvNARDYCDKTPIH 380
Ank_4 pfam13637
Ankyrin repeats (many copies);
1013-1065 9.72e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 9.72e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 62988328   1013 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL 1065
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
580-761 1.40e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.72  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192   91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328  706 EDVDGRTALSVAALcvPASKGHASVVSLLI------DRGAEVDHC-DKDGMTPLLVAAYEGHV 761
Cdd:cd22192  165 QDSLGNTVLHILVL--QPNKTFACQMYDLIlsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNI 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
979-1032 1.70e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    979 GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLI 1032
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
808-900 1.95e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.22  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   808 DSIDSEGRTVLSIA----SAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:PTZ00322   72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
                          90
                  ....*....|....*..
gi 62988328   884 FILASQEGHYDCVQILL 900
Cdd:PTZ00322  152 LELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
691-945 2.18e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   691 EIVEHLLDHGAEVNHEDVDGRTALSVAALcVPASKGHASVVSLLIDRgaEVDHCDKDGMTpllvAAYEGHVDVVDLLLEG 770
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLHIICK-EPNKLGMKEMIRSINKC--SVFYTLVAIKD----AFNNRNVEIFKIILTN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSID-SEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWT 849
Cdd:PHA02878  124 RYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   850 PLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPF-ILASQEGHYDCVQILLENKSNIDQRGY-DGRNALRVAALEghRD 927
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ER 281
                         250
                  ....*....|....*...
gi 62988328   928 IVELLFSHGADVNCKDAD 945
Cdd:PHA02878  282 KLKLLLEYGADINSLNSY 299
PHA02798 PHA02798
ankyrin-like protein; Provisional
624-907 2.52e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.39  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   624 TEVVSALLYAGVKVDCADADSRTAL-----RAAAWGGHEDIVLNLLQHGAEVNKADNEGRT---ALIAAAYMGHREIVEH 695
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   696 LLDHGAEVNHEDVDGRTALSVAalcvpASKGHA---SVVSLLIDRGAEVD-HCDKDGMTPLLVAAYEG----HVDVVDLL 767
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVY-----LQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLF 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   768 LEGGADVDHTDNNGRTPLLaaasmghaSVVNTLLFWGAAVDSidsegrtvlsiasaqgnveVVRTLLDRGLDENHRDDAG 847
Cdd:PHA02798  206 VDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKK-------------------NILDFIFSYIDINQVDELG 258
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   848 WTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02798  259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
PHA02878 PHA02878
ankyrin repeat protein; Provisional
927-1113 2.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   927 DIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAE-----------------------------------YF----- 965
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEmirsinkcsvfytlvaikdafnnrnveifkiiltnRYkniqt 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   966 -----------------------LENGANVEASDAE-GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAW 1021
Cdd:PHA02878  131 idlvyidkkskddiieaeitkllLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1022 QGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQE-GHIDVVQVLLEHGADPN-HADQFGRTAMRVAAKNghSQIIKLLEK 1099
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ERKLKLLLE 288
                         250
                  ....*....|....*.
gi 62988328  1100 YGA--SSLNGCSPSPV 1113
Cdd:PHA02878  289 YGAdiNSLNSYKLTPL 304
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
783-999 4.92e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.80  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  783 TPLLAAASMGHASVVNTLLfwgaAVDSID-----SEGRTVLSIASAQGNVEVVRTLLD--RGL-DENHRDD--AGWTPLH 852
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL----KCPSCDlfqrgALGETALHVAALYDNLEAAVVLMEaaPELvNEPMTSDlyQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  853 MAAFEGHRLICEALIEQGARTneidndgripfILASQEGHYdcvqiLLENKSNIdqrGYDGRNALRVAALEGHRDIVELL 932
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNL---IYYGEHPLSFAACVGNEEIVRLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  933 FSHGADVNCKDADGRPTLYILALENQLT----MAEYFLenganveASDAEGR-------------TALHVSCWQGHMEMV 995
Cdd:cd22192  156 IEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLIL-------SYDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMF 228

                 ....
gi 62988328  996 QVLI 999
Cdd:cd22192  229 QHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
578-631 5.39e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 5.39e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    578 GHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALL 631
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
645-697 6.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.00e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 62988328    645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
592-801 9.13e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 9.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   592 KVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAwgGHEDIVLN----LLQHG 667
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--GTDDEVIErinlLVQYG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   668 AEVNKA-DNEGRTALIAAAYMGHReIVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA02946  131 AKINNSvDEEGCGPLLACTDPSER-VFKKIMSIGFEARIVDKFGKNHIHRHLM---SDNPKASTISWMMKLGISPSKPDH 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328   747 DGMTPLLVAAYE--GHVDVVDLLLEgGADVDHTDNNGRTPL-LAAASMGHASVVNTLL 801
Cdd:PHA02946  207 DGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLtLLIKTLSPAHLINKLL 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
946-999 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    946 GRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLI 999
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
710-768 1.39e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328    710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLL 768
Cdd:pfam13637    1 ELTALHAAA-----ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
528-600 2.04e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 2.04e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328   528 IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02798 PHA02798
ankyrin-like protein; Provisional
927-1097 2.32e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 58.31  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   927 DIVELLFSHGADVNCKDAD-GRPTLYILA----LENQLTMAEYFLENGANVEASDAEGRTALHvscwqghmemvqvliay 1001
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEySTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY----------------- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1002 hadvnaadnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH---IDVVQVLLEHGADPN-HADQF 1077
Cdd:PHA02798  115 -------------CLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKE 181
                         170       180
                  ....*....|....*....|....
gi 62988328  1078 GRTAMRVAAKNGHSQ----IIKLL 1097
Cdd:PHA02798  182 KYDTLHCYFKYNIDRidadILKLF 205
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
844-948 2.42e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   844 DDAGWTPLHMAAFE-------GHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNA 916
Cdd:PTZ00322   72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
                          90       100       110
                  ....*....|....*....|....*....|..
gi 62988328   917 LRVAALEGHRDIVELLFSHGADVNCKDADGRP 948
Cdd:PTZ00322  152 LELAEENGFREVVQLLSRHSQCHFELGANAKP 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
962-1034 2.46e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 2.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328   962 AEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
480-639 2.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLD 559
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   560 VVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDG-WTALRSAAWGGHTEVVSALLYAGvkVD 638
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG--AD 227

                  .
gi 62988328   639 C 639
Cdd:PHA02875  228 C 228
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
929-1001 3.67e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 3.67e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62988328   929 VELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAY 1001
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
955-1110 4.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   955 LENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PHA02875   11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1035 GAVVDHTC-NQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAsSLN-----GC 1108
Cdd:PHA02875   91 GKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-CLDiedccGC 169

                  ..
gi 62988328  1109 SP 1110
Cdd:PHA02875  170 TP 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
549-631 4.99e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVS 628
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 62988328   629 ALL 631
Cdd:PTZ00322  166 LLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
710-903 8.06e-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: 56.94  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  710 GRTALSVAALcvpasKGHASVVSLLIDRGAEV--DHCDKD---GMTPLLVAAYEGHVDVVDLLLEGGADVdhtdNNGRtp 784
Cdd:cd22192   51 GETALHVAAL-----YDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSPR-- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  785 llAAASMGHASVVNTLLFwgaavdsidseGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLI-C 863
Cdd:cd22192  120 --ATGTFFRPGPKNLIYY-----------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFaC 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 62988328  864 EA---LIEQGARTNEI------DNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:cd22192  187 QMydlILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
959-1114 1.25e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA------------------YHADVNAA--------DNEK 1012
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFkiiltnryKNIQ 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1013 RSAL-----QSAAWQGHVKVVQLLIEHGAVVD-HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:PHA02878  130 TIDLvyidkKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209
                         170       180       190
                  ....*....|....*....|....*....|
gi 62988328  1087 KNGHSQIIKLLEKYGASS--LNGCSPSPVH 1114
Cdd:PHA02878  210 KHYNKPIVHILLENGASTdaRDKCGNTPLH 239
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
807-964 1.57e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 56.24  E-value: 1.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870  121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
                          170       180
                   ....*....|....*....|....*.
gi 62988328    939 VNCKDADGRPTLYILALENQLTmAEY 964
Cdd:TIGR00870  201 ILTADSLGNTLLHLLVMENEFK-AEY 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
789-866 1.90e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62988328   789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
847-900 2.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 2.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    847 GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILL 900
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
885-1066 2.98e-07

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: 55.19  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  885 ILASQEGHYDCVQILL---ENKSNIDQ--------RGYDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADG 946
Cdd:cd22193   37 LLNLNPGTNDTIRILLdiaEKTDNLKRfinaeytdEYYEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffQPKYQ 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  947 RPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGRTALHvscwqghmemvqvliayhADVNAADNEK-RSA 1015
Cdd:cd22193  117 GEGFYfgelplsLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH------------------ALVTVADNTKeNTK 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62988328 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22193  179 FVTRMYDMILIRGAKLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1002-1104 3.61e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1002 HADVNAADNekrsaLQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTA 1081
Cdd:PLN03192  520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
                          90       100
                  ....*....|....*....|...
gi 62988328  1082 MRVAAKNGHSQIIKLLEKYGASS 1104
Cdd:PLN03192  595 LWNAISAKHHKIFRILYHFASIS 617
Ank_5 pfam13857
Ankyrin repeats (many copies);
805-854 4.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 4.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 62988328    805 AAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMA 854
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
911-984 6.18e-07

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: 54.04  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  911 YDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADGRPTLY-------ILALENQLTMAEYFLEN---GANVE 973
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPGFYfgelplsLAACTNQLDIVKFLLENphsPADIS 171
                         90
                 ....*....|.
gi 62988328  974 ASDAEGRTALH 984
Cdd:cd22196  172 ARDSMGNTVLH 182
Semenogelin pfam05474
Semenogelin; This family consists of several mammalian secreted seminal proteins including ...
1210-1403 7.03e-07

Semenogelin; This family consists of several mammalian secreted seminal proteins including semenogelin I and II. Freshly ejaculated human semen has the appearance of a loose gel in which the predominant structural protein components are the seminal vesicle secreted semenogelins (Sg). This family also includes seminal vesicle secretory protein 3A from mouse, which has been shown to be involved in the coagulation of semen resulting in the formation of the copulatory plug.


Pssm-ID: 368458 [Multi-domain]  Cd Length: 582  Bit Score: 53.73  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   1361 --------------IMTNPNYHLQSNQvflgRVSVPRTMQDRGHQEVLEGYPSSETE 1403
Cdd:pfam05474  422 ekdvqkgvskgsisIQTEEKIHGKSQN----QVTIPSQDQEHGHKENKMSYQSSSTE 474
PHA02798 PHA02798
ankyrin-like protein; Provisional
992-1101 7.66e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.30  E-value: 7.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   992 MEMVQVLIAYHADVNAADNEKRSALQS-----AAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL- 1065
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTilsniKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 62988328  1066 --EHGADPNHADQFGRTAMRVAAKNGHS---QIIKLLEKYG 1101
Cdd:PHA02798  131 miENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
619-713 8.67e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   619 AWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLD 698
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
                          90
                  ....*....|....*
gi 62988328   699 HGAEvnHEDVDGRTA 713
Cdd:PTZ00322  170 HSQC--HFELGANAK 182
Ank_4 pfam13637
Ankyrin repeats (many copies);
611-664 9.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 9.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLL 664
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
1031-1085 1.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.05e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328   1031 LIEHGAV-VDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVA 1085
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
677-735 2.56e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.56e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328    677 GRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLI 735
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA-----ASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
887-932 2.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.88e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 62988328    887 ASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELL 932
Cdd:pfam13637    8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
663-717 2.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328    663 LLQHG-AEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
913-966 3.12e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 3.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFL 966
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
884-1086 3.54e-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: 51.62  E-value: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    884 FILASQEGHYDCVQILLEN--KSNIDQRGYDGRNALRVAALEG-HRDIVELLFSHgadvNCKDADGRPTLYILALENQ-- 958
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEpkKLNINCPDRLGRSALFVAAIENeNLELTELLLNL----SCRGAVGDTLLHAISLEYVda 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    959 -----LTMAEYFLENGANVEASD------AEGRTALHVSCWQGHMEMVQVLIAYHADVNAA---DNEKRSALQSAAWQGh 1024
Cdd:TIGR00870   97 veailLHLLAAFRKSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHG- 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   1025 vkvvqlliEHgavvdhtcnqgatALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:TIGR00870  176 --------ES-------------PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
PHA02946 PHA02946
ankyin-like protein; Provisional
654-973 3.76e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.21  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   654 GGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAlcvPASKGHASVVSL 733
Cdd:PHA02946   49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS---GTDDEVIERINL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   734 LIDRGAEVDH-CDKDGMTPLLvAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA--AASMGHASVVNTLLFWGAAVDSI 810
Cdd:PHA02946  126 LVQYGAKINNsVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKP 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   811 DSEGRTVLSIASAQ--GNVEVVRTLLDrGLDENHRDDAGWTPLHMAAfegHRLICEALIEQGARTNEIDNDGRIPFILAS 888
Cdd:PHA02946  205 DHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLI---KTLSPAHLINKLLSTSNVITDQTVNICIFY 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   889 QEGhyDCVQILlenksNIDQRGYDGRNaLRVAALEGHRDIVELLFSHgaDVNCKDAdgrptLYILALENQLTMAEYFLEN 968
Cdd:PHA02946  281 DRD--DVLEII-----NDKGKQYDSTD-FKMAVEVGSIRCVKYLLDN--DIICEDA-----MYYAVLSEYETMVDYLLFN 345

                  ....*
gi 62988328   969 GANVE 973
Cdd:PHA02946  346 HFSVD 350
Ank_5 pfam13857
Ankyrin repeats (many copies);
966-1019 4.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 4.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 62988328    966 LENG-ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSA 1019
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
747-779 4.51e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 4.51e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 62988328    747 DGMTPLLVAAYE-GHVDVVDLLLEGGADVDHTDN 779
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
839-1066 4.89e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 51.03  E-value: 4.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  839 DENHRDDAGWTPLHMAAFEGH--RLICEALIEQGARtneiDNDGRIPFILASQEGHYdcvqillenksnidqrgYDGRNA 916
Cdd:cd21882   18 SAYQRGATGKTCLHKAALNLNdgVNEAIMLLLEAAP----DSGNPKELVNAPCTDEF-----------------YQGQTA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  917 LRVAALEGHRDIVELLFSHGADVN---CKDA---DGRPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGR 980
Cdd:cd21882   77 LHIAIENRNLNLVRLLVENGADVSaraTGRFfrkSPGNLFYfgelplsLAACTNQEEIVRLLLENGaqpAALEAQDSLGN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  981 TALHVscwqghmemvQVLIAYhadvNAADNEKRSalqsaawqghVKVVQLLIEHGAVVDHTC-------NQGATALCIAA 1053
Cdd:cd21882  157 TVLHA----------LVLQAD----NTPENSAFV----------CQMYNLLLSYGAHLDPTQqleeipnHQGLTPLKLAA 212
                        250
                 ....*....|...
gi 62988328 1054 QEGHIDVVQVLLE 1066
Cdd:cd21882  213 VEGKIVMFQHILQ 225
PHA02798 PHA02798
ankyrin-like protein; Provisional
526-801 5.44e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   526 DSIRTLLDNGASVNQCDSNGR----TLLAN-AAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTlaarqghtkvvnCLIGC 600
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYStplcTILSNiKDYKHMLDIVKILIENGADINKKNSDGETPLY------------CLLSN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   601 GAnINhtdqdgwtalrsaawggHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADN-E 676
Cdd:PHA02798  120 GY-IN-----------------NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNkE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   677 GRTALiaAAYMGHR------EIVEHLLDHGAEVNHEDVDGRTAL--SVAALCVPASKGHASVVSLLIdrgAEVDHCDKD- 747
Cdd:PHA02798  182 KYDTL--HCYFKYNidridaDILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNKRFKKNILDFIF---SYIDINQVDe 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   748 -GMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLL 801
Cdd:PHA02798  257 lGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSIL 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
513-565 1.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    513 RTSCIVRQA-LEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLV 565
Cdd:pfam13637    1 ELTALHAAAaSGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
545-598 1.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62988328    545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLI 598
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
531-585 1.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328    531 LLDNG-ASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLA 585
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
978-1010 1.27e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 62988328    978 EGRTALHVSCWQ-GHMEMVQVLIAYHADVNAADN 1010
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
734-785 2.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 62988328    734 LIDRG-AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL 785
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
896-957 2.88e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   896 VQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRpTLYILALEN 957
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEEN 158
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
1044-1072 2.93e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.93e-05
                            10        20
                    ....*....|....*....|....*....
gi 62988328    1044 QGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
676-707 2.99e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 42.28  E-value: 2.99e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328    676 EGRTAL-IAAAYMGHREIVEHLLDHGAEVNHED 707
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
1046-1102 3.38e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 3.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328  1046 ATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGA 1102
Cdd:PTZ00322   83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
1044-1075 3.68e-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: 41.89  E-value: 3.68e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328   1044 QGATALCIAA-QEGHIDVVQVLLEHGADPNHAD 1075
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
1025-1102 5.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1025 VKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHI-----DVVQVLLEHGADPNHADQFGRTAMRVAA--KNGHSQIIKLL 1097
Cdd:PHA03100   48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127

                  ....*
gi 62988328  1098 EKYGA 1102
Cdd:PHA03100  128 LDNGA 132
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
747-775 6.11e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 6.11e-05
                            10        20
                    ....*....|....*....|....*....
gi 62988328     747 DGMTPLLVAAYEGHVDVVDLLLEGGADVD 775
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
830-1097 6.20e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 6.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   830 VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP--FILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   908 QRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTL--YILALENQLTMAEYFLENGANVEASDAEGRTALHV 985
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   986 SCWQ--GHMEMVQVLIAyHADVNAADNEKRSALQ---SAAWQGHVkVVQLLIEHGAVVDHTCNqgataLCIAAQEGhiDV 1060
Cdd:PHA02946  215 VCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTlliKTLSPAHL-INKLLSTSNVITDQTVN-----ICIFYDRD--DV 285
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 62988328  1061 VQVLLEHGadpnhaDQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA02946  286 LEIINDKG------KQYDSTDFKMAVEVGSIRCVKYL 316
PHA02859 PHA02859
ankyrin repeat protein; Provisional
495-613 6.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   495 EVLQLLVKAGAHVN--SEDDRTSCI-----VRQALErEDSIRTLLDNGASVNQCDSNGRTLLAN--AAYSGSLDVVNLLV 565
Cdd:PHA02859   67 EILKFLIENGADVNfkTRDNNLSALhhylsFNKNVE-PEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLI 145
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 62988328   566 SRGADLEIEDAHG----HTPLTLAARQghtKVVNCLIGCGANINHTDQDGWT 613
Cdd:PHA02859  146 DSGVSFLNKDFDNnnilYSYILFHSDK---KIFDFLTSLGIDINETNKSGYN 194
Ank_5 pfam13857
Ankyrin repeats (many copies);
766-821 8.47e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 8.47e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328    766 LLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIA 821
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
676-704 1.05e-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: 40.65  E-value: 1.05e-04
                            10        20
                    ....*....|....*....|....*....
gi 62988328     676 EGRTALIAAAYMGHREIVEHLLDHGAEVN 704
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
747-776 1.13e-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: 40.32  E-value: 1.13e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 62988328    747 DGMTPLLVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
663-734 1.15e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328   663 LLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLL 734
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA-----EENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
577-605 1.25e-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: 40.26  E-value: 1.25e-04
                            10        20
                    ....*....|....*....|....*....
gi 62988328     577 HGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
978-1007 1.38e-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: 40.26  E-value: 1.38e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 62988328     978 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
899-954 1.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328    899 LLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGrPTLYILA 954
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
584-674 1.55e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   584 LAArQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNL 663
Cdd:PTZ00322   89 LAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
                          90
                  ....*....|.
gi 62988328   664 LQHGAEVNKAD 674
Cdd:PTZ00322  168 SRHSQCHFELG 178
PHA02874 PHA02874
ankyrin repeat protein; Provisional
497-609 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   497 LQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANA-AYSGSLDVVNLLVSRGADLEIED 575
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKD 285
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 62988328   576 AHGHTPLTLAARQ-GHTKVVNCLIGCGANINHTDQ 609
Cdd:PHA02874  286 NKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
978-1007 2.44e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 2.44e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 62988328    978 EGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
710-857 2.65e-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: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  710 GRTALSVAALcvpasKGHASVVSLLIDRGAEVD-------------HCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd21882   73 GQTALHIAIE-----NRNLNLVRLLVENGADVSaratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaa 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDSIDS-------EGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd21882  148 LEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRE 227
                        170       180
                 ....*....|....*....|....*.
gi 62988328  838 LDENH----RDDAGWT--PLHMAAFE 857
Cdd:cd21882  228 FSGPYqplsRKFTEWTygPVTSSLYD 253
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
691-862 2.73e-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: 45.52  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  691 EIVEHLL----DHG-------AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKD------------ 747
Cdd:cd22194  111 EIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAI-----ERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegf 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  748 --GMTPLLVAAYEGHVDVVDLLLEggadvdhtdnNGRTPLLAAASMGhasvvNTLLFwgAAVD-SIDSEGRTVLSIasaQ 824
Cdd:cd22194  186 yfGETPLALAACTNQPEIVQLLME----------KESTDITSQDSRG-----NTVLH--ALVTvAEDSKTQNDFVK---R 245
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 62988328  825 GNVEVVRTLLDRGLdENHRDDAGWTPLHMAAFEGHRLI 862
Cdd:cd22194  246 MYDMILLKSENKNL-ETIRNNEGLTPLQLAAKMGKAEI 282
PHA02859 PHA02859
ankyrin repeat protein; Provisional
658-784 2.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   658 DIVLNLLQHGAEVN-KADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSVaALCVPASKghASVV 731
Cdd:PHA02859   67 EILKFLIENGADVNfKTRDNNLSAL--HHYLSFNknvepEILKILIDSGSSITEEDEDGKNLLHM-YMCNFNVR--INVI 141
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62988328   732 SLLIDRGAEVDHCDKDGmTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA02859  142 KLLIDSGVSFLNKDFDN-NNILYSYILFHSDkkIFDFLTSLGIDINETNKSGYNC 195
PHA02989 PHA02989
ankyrin repeat protein; Provisional
492-717 2.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.12  E-value: 2.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   492 KEQEVLQLLVKAGAHVNSED-DRTSCIV----RQALEREDSIRTLLDNGASVNQC-DSNGRTLLAN--AAYSGSLDVVNL 563
Cdd:PHA02989   86 KIKKIVKLLLKFGADINLKTfNGVSPIVcfiyNSNINNCDMLRFLLSKGINVNDVkNSRGYNLLHMylESFSVKKDVIKI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   564 LVSRGAD-LEIEDAHGHTPLTLAARQG----HTKVVNCLIGCGANINHTDQdgwtalrsaawgGHTEVVSALLyagvkvd 638
Cdd:PHA02989  166 LLSFGVNlFEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNN------------GSESVLESFL------- 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62988328   639 cadaDSRTALRAaawggHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:PHA02989  227 ----DNNKILSK-----KEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
885-1066 2.89e-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: 45.23  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  885 ILASQEGHYDCVQILLEnksnIDQRG---------------YDGRNALRVAALEGHRDIVELLFSHGADVNCKDAD---- 945
Cdd:cd22197   55 VLNLQDGVNACIMPLLE----IDKDSgnpkplvnaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffq 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  946 ---------GRPTLYILALENQLTMAEYFLENG---ANVEASDAEGRTALhvscwqghmemvqvliayHADVNAADN-EK 1012
Cdd:cd22197  131 kkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVL------------------HALVMIADNsPE 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62988328 1013 RSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22197  193 NSALVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
499-577 3.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   499 LLVKAGAHVNSEDDRTSCIVRQAL--EREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDA 576
Cdd:PHA03100  177 YLLSYGVPINIKDVYGFTPLHYAVynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                  .
gi 62988328   577 H 577
Cdd:PHA03100  257 T 257
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
912-941 3.54e-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: 3.54e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 62988328     912 DGRNALRVAALEGHRDIVELLFSHGADVNC 941
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
959-1095 3.77e-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: 45.13  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  959 LTMAEyflENG-------ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAAD-----NEK---------RSALQ 1017
Cdd:cd22194  117 LAFAE---ENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffNPKykhegfyfgETPLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328 1018 SAAWQGHVKVVQLLIEH----GAVVDHTCNQGATALCIAAQ--EGHIDVV-----QVLLEHG-----ADPNHAdqfGRTA 1081
Cdd:cd22194  194 LAACTNQPEIVQLLMEKestdITSQDSRGNTVLHALVTVAEdsKTQNDFVkrmydMILLKSEnknleTIRNNE---GLTP 270
                        170
                 ....*....|....
gi 62988328 1082 MRVAAKNGHSQIIK 1095
Cdd:cd22194  271 LQLAAKMGKAEILK 284
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
577-608 3.77e-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: 3.77e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328    577 HGHTPLTLAA-RQGHTKVVNCLIGCGANINHTD 608
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
847-878 5.76e-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: 5.76e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328    847 GWTPLHMAA-FEGHRLICEALIEQGARTNEIDN 878
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
720-858 6.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 6.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   720 CVPASKGHASVVSLLIDRGAEVDHCDKD-GMTPL---LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL---LAAASMg 792
Cdd:PHA02859   58 CLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV- 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   793 HASVVNTLLFWGAAVDSIDSEGRTVL-SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEG 858
Cdd:PHA02859  137 RINVIKLLIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
912-943 6.23e-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: 6.23e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328    912 DGRNALRVAALE-GHRDIVELLFSHGADVNCKD 943
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
709-746 6.54e-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: 6.54e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 62988328    709 DGRTALSVAAlcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:pfam00023    1 DGNTPLHLAA----GRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
696-755 7.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62988328    696 LLDHG-AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA-----KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
577-606 7.19e-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: 38.39  E-value: 7.19e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 62988328    577 HGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
908-1084 8.03e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.72  E-value: 8.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  908 QRGYDGRNALRVAAL---EGHRDIVELLFshgadvnckDADgRPTLYILALENQLTMAEYFlenganveasdaEGRTALH 984
Cdd:cd21882   21 QRGATGKTCLHKAALnlnDGVNEAIMLLL---------EAA-PDSGNPKELVNAPCTDEFY------------QGQTALH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  985 VSCWQGHMEMVQVLIAYHADVNAADNekrsalqSAAWQGHvkvvqlliehgavvDHTCNQ-GATALCIAAQEGHIDVVQV 1063
Cdd:cd21882   79 IAIENRNLNLVRLLVENGADVSARAT-------GRFFRKS--------------PGNLFYfGELPLSLAACTNQEEIVRL 137
                        170       180
                 ....*....|....*....|....
gi 62988328 1064 LLEHGADP---NHADQFGRTAMRV 1084
Cdd:cd21882  138 LLENGAQPaalEAQDSLGNTVLHA 161
PHA02875 PHA02875
ankyrin repeat protein; Provisional
481-573 9.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   481 PVRDSLSTL----IPKEQEVLQLLVKAGAHVNSED--DRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGR-TLLANAA 553
Cdd:PHA02875  131 PNTDKFSPLhlavMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210
                          90       100
                  ....*....|....*....|
gi 62988328   554 YSGSLDVVNLLVSRGADLEI 573
Cdd:PHA02875  211 ENNKIDIVRLFIKRGADCNI 230
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
676-705 9.56e-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: 38.01  E-value: 9.56e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 62988328    676 EGRTALIAAAYMGHREIVEHLLDHGAEVNH 705
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
826-940 1.13e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   826 NVEVVRTLLDRGLDENHR-DDAGWTPLHmaafegHRL---------ICEALIEQGARTNEIDNDGRIPF--ILASQEGHY 893
Cdd:PHA02859   65 NVEILKFLIENGADVNFKtRDNNLSALH------HYLsfnknvepeILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 62988328   894 DCVQILLENKSNIDQRGYDGRNALRVAAL-EGHRDIVELLFSHGADVN 940
Cdd:PHA02859  139 NVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDIN 186
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
912-941 1.53e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 62988328    912 DGRNALRVAALEGHRDIVELLFSHGADVNC 941
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
22-195 1.65e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.95  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328     22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328    102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 62988328    175 LPllgmKPPQQSLYLLVDSVD 195
Cdd:pfam13191  126 LL----ARGERPLVLVLDDLQ 142
PHA02946 PHA02946
ankyin-like protein; Provisional
1026-1110 1.66e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  1026 KVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQI--IKLLEKYGAS 1103
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAK 132
                          90
                  ....*....|..
gi 62988328  1104 SLN-----GCSP 1110
Cdd:PHA02946  133 INNsvdeeGCGP 144
PHA02795 PHA02795
ankyrin-like protein; Provisional
538-589 1.81e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 42.67  E-value: 1.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 62988328   538 VNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQG 589
Cdd:PHA02795  214 INQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
710-869 2.45e-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: 42.17  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  710 GRTALSVAALCVpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-----------VDVVDLLLEGGADVdHTD 778
Cdd:cd21882   26 GKTCLHKAALNL--NDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADV-SAR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  779 NNGRT--------------PLLAAASMGHASVVNTLLFWG---AAVDSIDSEGRTVLSIASAQGNVEVVRTLL------- 834
Cdd:cd21882  103 ATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFvcqmynl 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 62988328  835 ----DRGLDE--------NHRddaGWTPLHMAAFEGHRLICEALIEQ 869
Cdd:cd21882  183 llsyGAHLDPtqqleeipNHQ---GLTPLKLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
833-887 2.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.93e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 62988328    833 LLDRG-LDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
780-811 3.38e-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: 3.38e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 62988328    780 NGRTPL-LAAASMGHASVVNTLLFWGAAVDSID 811
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
545-615 3.60e-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: 41.92  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDA--------------HGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                 ....*
gi 62988328  611 GWTAL 615
Cdd:cd22192  169 GNTVL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
492-588 4.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   492 KEQEVLQLLVKAGAHVNSEDDRTSCIVRQALE--REDSIRTLLDNGASVNQCDSNGRTLL-------------------- 549
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhyNKPIVHILLENGASTDARDKCGNTPLhisvgyckdydilklllehg 258
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 62988328   550 --ANAAYS-----------GSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQ 588
Cdd:PHA02878  259 vdVNAKSYilgltalhssiKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
1025-1101 5.13e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 5.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328  1025 VKVVQLLIEHGAvvDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYG 1101
Cdd:PLN03192  507 LNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
PHA02795 PHA02795
ankyrin-like protein; Provisional
992-1100 5.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.13  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   992 MEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEG--------HIDVVQV 1063
Cdd:PHA02795  201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 62988328  1064 LLEhgaDPNHADQFGRTAMRVAAKNghSQIIKLLEKY 1100
Cdd:PHA02795  281 LLR---EPLSIDCIKLAILNNTIEN--HDVIKLCIKY 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
847-871 5.50e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 5.50e-03
                           10        20
                   ....*....|....*....|....*
gi 62988328    847 GWTPLHMAAFEGHRLICEALIEQGA 871
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGA 26
PHA02795 PHA02795
ankyrin-like protein; Provisional
708-812 5.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.75  E-value: 5.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   708 VDGRTALSVAALCVPASKghasvvsllidrgaEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 787
Cdd:PHA02795  195 VDEPTVLEIYKLCIPYIE--------------DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDV 260
                          90       100       110
                  ....*....|....*....|....*....|...
gi 62988328   788 AASMG--------HASVVNTLLFWGAAVDSIDS 812
Cdd:PHA02795  261 AVDRGsviarretHLKILEILLREPLSIDCIKL 293
PHA02859 PHA02859
ankyrin repeat protein; Provisional
493-584 6.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   493 EQEVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLAN-AAYSGSLDVVNLLVSR 567
Cdd:PHA02859  102 EPEILKILIDSGSSITEEDEDGKNLLHMYMCnfnvRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSL 181
                          90
                  ....*....|....*..
gi 62988328   568 GADLEIEDAHGHTPLTL 584
Cdd:PHA02859  182 GIDINETNKSGYNCYDL 198
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
682-852 6.57e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   682 IAAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASkghASVVSLLIDRGAEVDHCDKDGMTPLLvaAY 757
Cdd:PHA02716  180 ILHAYLGNMyvdiDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVC---ASVIKKIIELGGDMDMKCVNGMSPIM--TY 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   758 EGHVDVVDLLLEgGADVDHTDNNGRT--PLLAAASMGHA-----SVVNTLLFWGAAVDSIDSEGRTVLS--IASAQGNVE 828
Cdd:PHA02716  255 IINIDNINPEIT-NIYIESLDGNKVKniPMILHSYITLArnidiSVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTD 333
                         170       180
                  ....*....|....*....|....
gi 62988328   829 VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA02716  334 IIKLLHEYGNDLNEPDNIGNTVLH 357
PHA02795 PHA02795
ankyrin-like protein; Provisional
669-777 6.70e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.75  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   669 EVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA---ALCVPASKGHASVVSLLIDRGAEVDhCD 745
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAvdrGSVIARRETHLKILEILLREPLSID-CI 291
                          90       100       110
                  ....*....|....*....|....*....|..
gi 62988328   746 KdgmTPLLVAAYEGHvDVVDLLLEGGADVDHT 777
Cdd:PHA02795  292 K---LAILNNTIENH-DVIKLCIKYFMMVDYS 319
PHA02859 PHA02859
ankyrin repeat protein; Provisional
927-1047 6.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 6.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   927 DIVELLFSHGADVNCKDADGRPTL---YILALEN-QLTMAEYFLENGANVEASDAEGRTALHV--SCWQGHMEMVQVLIA 1000
Cdd:PHA02859   67 EILKFLIENGADVNFKTRDNNLSAlhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLID 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 62988328  1001 YHADVNAADNEKRSALQS-AAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02859  147 SGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYN 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
879-907 6.96e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 6.96e-03
                            10        20
                    ....*....|....*....|....*....
gi 62988328     879 DGRIPFILASQEGHYDCVQILLENKSNID 907
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
710-843 7.15e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 7.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEV-------------DHCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd22197   94 GHSALHIAI-----EKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpas 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDS-------IDSEGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd22197  169 LQAQDSLGNTVLHALVMIADNSPENSalvikmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQRE 248

                 ....*.
gi 62988328  838 LDENHR 843
Cdd:cd22197  249 FSGPYQ 254
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
865-1066 7.72e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  865 ALIEQGARTNEIdndgrIPFILASQEGHyDCVQILLEnkSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKdA 944
Cdd:cd22194  101 ALLNINENTKEI-----VRILLAFAEEN-GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH-A 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328  945 DGR---PT------------LYILALENQLTMAEYFLENGANVEAS-DAEGRTALhvscwqghmemvqvliayHADVNAA 1008
Cdd:cd22194  172 KGVffnPKykhegfyfgetpLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVL------------------HALVTVA 233
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62988328 1009 DNekrsalqSAAWQGHVKVV--QLLIEHG--AVVDHTCNQGATALCIAAQEGHIDVVQVLLE 1066
Cdd:cd22194  234 ED-------SKTQNDFVKRMydMILLKSEnkNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
730-941 7.79e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   730 VVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHV--DVVDLLLEGGADVDHTDNNGRTPLLAaaSMGHASVVNTLLFwGAAV 807
Cdd:PHA02716  194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPIMT--YIINIDNINPEIT-NIYI 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   808 DSIDSEGRT------VLSIASAQG-NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEgHRL---ICEALIEQGARTNEID 877
Cdd:PHA02716  271 ESLDGNKVKnipmilHSYITLARNiDISVVYSFLQPGVKLHYKDSAGRTCLHQYILR-HNIstdIIKLLHEYGNDLNEPD 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62988328   878 NDGRIpfILASQEGHYDCVQILlenKSNIDqrgydgrNALRVaaleghrDIVELLFSHGAD---VNC 941
Cdd:PHA02716  350 NIGNT--VLHTYLSMLSVVNIL---DPETD-------NDIRL-------DVIQCLISLGADitaVNC 397
PHA02989 PHA02989
ankyrin repeat protein; Provisional
894-985 8.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.49  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   894 DCVQILLENKSNIDQRGYDGR---NALRVAALEGH--RDIVELLFSHGADVNCKDADGRPTLYILALE---NQLTMAEYF 965
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGYIETplcAVLRNREITSNkiKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
                          90       100
                  ....*....|....*....|.
gi 62988328   966 LENGANV-EASDAEGRTALHV 985
Cdd:PHA02989  131 LSKGINVnDVKNSRGYNLLHM 151
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
729-851 8.55e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62988328   729 SVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMghASVVNTLlfwgaa 806
Cdd:PHA02716  298 SVVYSFLQPGVKLHYKDSAGRTCLhqYILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSM--LSVVNIL------ 369
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 62988328   807 vdsiDSEGRTVLsiasaqgNVEVVRTLLDRGLDENHRDDAGWTPL 851
Cdd:PHA02716  370 ----DPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPL 403
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
645-675 9.51e-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: 9.51e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 62988328    645 RTAL-RAAAWGGHEDIVLNLLQHGAEVNKADN 675
Cdd:pfam00023    3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
1064-1103 9.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 9.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 62988328   1064 LLEHG-ADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS 1103
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD 41
 
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.
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