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Conserved domains on  [gi|1034640726|ref|XP_016863960|]
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ankyrin repeat domain-containing protein 50 isoform X1 [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 1034640726  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666    161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034640726  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 1034640726  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100   157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034640726  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 1034640726 1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726 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 1034640726   22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 1034640726  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 1034640726  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666    161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034640726  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 1034640726  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA03095   183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876   240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  922 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PHA02876   316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  995 VQVLIAYHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 1072
Cdd:PHA02876   391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                          330       340       350
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  983 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 1062
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726 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 1034640726  752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1034640726  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 1034640726  495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100   157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 942
Cdd:cd22192      7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 1015
Cdd:cd22192     71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 1067
Cdd:cd22192    129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
                          250       260
                   ....*....|....*....|....*.
gi 1034640726 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 1034640726  580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192     91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034640726  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 1034640726  807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870  121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
                          170       180
                   ....*....|....*....|....*.
gi 1034640726  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 1034640726 1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726 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 1034640726  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 1034640726  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 1034640726   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 1034640726   22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 1034640726  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 1034640726  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  638 DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA 717
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  718 alcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:COG0666    161 -----AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034640726  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 1034640726  629 ALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDV 708
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  709 DGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA 788
Cdd:COG0666     86 GGNTLLHAAA-----RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  789 ASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIE 868
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  833 LLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYD 912
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  913 GRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHM 992
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  993 EMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPN 1072
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  531 LLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  611 GWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHR 690
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  691 EIVEHLLDHGAEVNHEDVDGRTALSVAalcvpASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEG 770
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLA-----AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  861 LICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVN 940
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  941 CKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAA 1020
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1021 WQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKY 1100
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                   ..
gi 1034640726 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 1034640726  728 ASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAV 807
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  808 DSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILA 887
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  888 SQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLE 967
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  495 EVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:COG0666     37 LLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  575 DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWG 654
Cdd:COG0666    117 DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  655 GHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpasKGHASVVSLL 734
Cdd:COG0666    197 GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA-----AGAALIVKLL 271
                          250
                   ....*....|....*...
gi 1034640726  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 1034640726  707 DVDGRTALSVAALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLL 786
Cdd:COG0666     13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  787 AAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEAL 866
Cdd:COG0666     93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  867 IEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADG 946
Cdd:COG0666    173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  804 GAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  884 FILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCN 1043
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034640726 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 1034640726  761 VDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  841 NHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  921 ALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA 1000
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1034640726 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 1034640726  443 QAKNLTPLEAQEFALHLINSNLQLETAELALWMIWNGTPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQAL 522
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  523 E--REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGC 600
Cdd:COG0666     96 RngDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  601 GANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTA 680
Cdd:COG0666    176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1034640726  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 1034640726  625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADNEGRTALIAaaYMGH---REIVEHLLD 698
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL--YLYNattLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  699 HGAEVNHEDVDGRTALSVAaLCVPASkgHASVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDH 776
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVY-LSGFNI--NPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYA 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  777 TDNNGRTPL--LAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVE--VVRTLLDRGLDENHRDDAGWTPLH 852
Cdd:PHA03095   183 VDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLH 262
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  524 REDSIRTLLDNGASVNQCDSNGRTLLA---NAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHT-KVVNCLIG 599
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  600 CGANINHTDQDGWTALrsaawggHTevvsallYAGVKvdcadadsRTalraaawggHEDIVLNLLQHGAEVNKADNEGRT 679
Cdd:PHA03095   106 AGADVNAKDKVGRTPL-------HV-------YLSGF--------NI---------NPKVIRLLLRKGADVNALDLYGMT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  680 ALiaAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA 755
Cdd:PHA03095   155 PL--AVLLKSRnanvELLRLLIDAGADVYAVDDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  756 AYEGHVD--VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTL 833
Cdd:PHA03095   230 ATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAA 309

                   ...
gi 1034640726  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 1034640726  558 LDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKV 637
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  638 DCADADSRTALRaaawggHEDIVLNLLQH--GAEVNKADNEGRTALIAAAYMGH-REIVEHLLDHGAEVNHEDVDGRTAL 714
Cdd:PHA02876   238 NKNDLSLLKAIR------NEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  715 SVAalcvpASKGHASV-VSLLIDRGAEVDHCDKDGMTPLLVAA-YEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMG 792
Cdd:PHA02876   312 YLM-----AKNGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  793 HASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEV-VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-ICEALIEQG 870
Cdd:PHA02876   387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNG 466
                          330       340       350
                   ....*....|....*....|....*....|
gi 1034640726  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 1034640726  686 YMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PHA02874    10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAI----RSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  766 LLLEGGADvdhtdnngrTPLLAAASMgHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDD 845
Cdd:PHA02874    86 LLIDNGVD---------TSILPIPCI-EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  846 AGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEgH 925
Cdd:PHA02874   156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-N 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  926 RDIVELLFSHgADVNCKDADG-RPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSC-WQGHMEMVQVLIAYHA 1003
Cdd:PHA02874   235 RSAIELLINN-ASINDQDIDGsTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAV 313
                          330
                   ....*....|.
gi 1034640726 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 1034640726  763 VVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENH 842
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  843 RDDAGWTPLHMAAFEGHRLiceaLIEQGARTNEIDNDGRIPFILASQEGHYD-CVQILLENKSNIDQRGYDGRNALRVAA 921
Cdd:PHA02876   240 NDLSLLKAIRNEDLETSLL----LYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  922 LEGH-RDIVELLFSHGADVNCKDadgrpTLYILALENQLTMAEY------FLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PHA02876   316 KNGYdTENIRTLIMLGADVNAAD-----RLYITPLHQASTLDRNkdivitLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  995 VQVLIAYHADVNAADNEKRSALQSAAWQGHVKV-VQLLIEHGAVVDHTCNQGATALCIAAQEG-HIDVVQVLLEHGADPN 1072
Cdd:PHA02876   391 INTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                          330       340       350
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSeddRTSC-------IVRQAlEREDSIRTLLDNGASVNQCDSNGRTLLAna 552
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIVRLLLEAGADVNA---PERCgftplhlYLYNA-TTLDVIKLLIKAGADVNAKDKVGRTPLH-- 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  553 AYSGSL----DVVNLLVSRGADLEIEDAHGHTPLT--LAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHT-- 624
Cdd:PHA03095   123 VYLSGFninpKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHED--IVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA03095   203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282
                          250
                   ....*....|....*
gi 1034640726  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 1034640726  557 SLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGH---TKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTE-VVSALLY 632
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  633 AGVKVDCADADSRTALRAAAWGG--HEDIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR----EIVEHLLDHGAEVNHE 706
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRnanvELLRLLIDAGADVYAV 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  707 DVDGRTALSVAALCVpasKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVD--VVDLLLEGGADVDHTDNNGRTP 784
Cdd:PHA03095   184 DDRFRSLLHHHLQSF---KPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTP 260
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  862 ICEALIEQGARTNEIDNDGRIPFILASQEGHydcvqillenksnidqrgydgrNALRVaaleghRDIVELLFSHGADVNC 941
Cdd:PHA03100    50 VVKILLDNGADINSSTKNNSTPLHYLSNIKY----------------------NLTDV------KEIVKLLLEYGANVNA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  942 KDADGRPTLYILALE--NQLTMAEYFLENGANVEASDAEGRTALH--VSCWQGHMEMVQVLIAYHADVNAADNekrsalq 1017
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHlyLESNKIDLKILKLLIDKGVDINAKNR------- 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1018 saawqghvkvVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLL 1097
Cdd:PHA03100   175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                   ....*.
gi 1034640726 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 1034640726  658 DIVLNLLQHGAEVNKADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSvaalCVPASKGHASVVS 732
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPL--HLYLHYSsekvkDIVRLLLEAGADVNAPERCGFTPLH----LYLYNATTLDVIK 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  733 LLIDRGAEVDHCDKDGMTPLLV--AAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASV--VNTLLFWGAAVD 808
Cdd:PHA03095   102 LLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVY 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  809 SIDSEGRTVLSI--ASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHrliCEALIEQgartneidndgriPFIL 886
Cdd:PHA03095   182 AVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVL-------------PLLI 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  887 AsqeghydcvqillenksnidqrgydgrnalrvaaleghrdivellfshGADVNCKDADGRPTLYILALENQLTMAEYFL 966
Cdd:PHA03095   246 A------------------------------------------------GISINARNRYGQTPLHYAAVFNNPRACRRLI 277
                          330
                   ....*....|....*..
gi 1034640726  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 1034640726  820 IASAQGNVEVVRTLLDRGLDENHRDDAGWTPLH--MAAFEGHRL-ICEALIEQGARTNEIDNDGRIPFIL----ASQEgh 892
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLylynATTL-- 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  893 yDCVQILLENKSNIDQRGYDGRNALRV--AALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMA--EYFLEN 968
Cdd:PHA03095    98 -DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  969 GANVEASDAEGRTALHVscwqgHME-------MVQVLIAYHADVNAADNEKRSALQSAAWQGHVK--VVQLLIEHGAVVD 1039
Cdd:PHA03095   177 GADVYAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISIN 251
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034640726 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 1034640726  625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHE-----DIVLNLLQHGAEVNKADNEGRTALIAAAY--MGHREIVEHLL 697
Cdd:PHA03100    49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  698 DHGAEVNHEDVDGRTALSVAALCVPASKghaSVVSLLIDRGAEVDHCDKdgmtpllvaayeghvdvVDLLLEGGADVDHT 777
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNKIDL---KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  606 HTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAA 685
Cdd:PLN03192   520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  686 YMGHREIVeHLLDHGAEVNHEDVDGRTalsvaaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVD 765
Cdd:PLN03192   600 SAKHHKIF-RILYHFASISDPHAAGDL------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  492 KEQEVLQLLVKA-GAHVNSEDDRTSCIVRQALEREDS--IRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRG 568
Cdd:PHA02874    12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAkiVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  569 ADLEIedahghtpltLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTAL 648
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  649 RAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpaskGHA 728
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII------HNR 235
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034640726  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 1034640726  983 LHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDhtCNQGATALCIAAQEGHIDVVQ 1062
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726 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 1034640726  826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRL-----ICEALIEQGARTNEIDNDGRIP-FILASQE-GHYDCVQI 898
Cdd:PHA03100    47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPlLYAISKKsNSYSIVEY 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  899 LLENKSNIDQRGYDGRNALRVAALEGHRD--IVELLFSHGADVNCKDAdgrptlyilalenqltmAEYFLENGANVEASD 976
Cdd:PHA03100   127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  851 LHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKsNIDQRGYdGRNALRVAALEGHRDIVE 930
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726  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 1034640726  718 ALCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVV 797
Cdd:PHA02875     5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  798 NTLLFWGA-AVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEI 876
Cdd:PHA02875    85 EELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  761 VDVVDLLLEGGADvdHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGLDE 840
Cdd:PLN03192   507 LNVGDLLGDNGGE--HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  841 NHRDDAGWTPLHMAAFEGHRLICEALiEQGARTNEIDNDGRIpFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVA 920
Cdd:PLN03192   585 HIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
                          170       180
                   ....*....|....*....|....*
gi 1034640726  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 1034640726  752 LLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLfwgAAVDS-IDSEGRTVLSIASAQGNVEVV 830
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVnLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1034640726  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 1034640726  891 GHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEngA 970
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD--L 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  971 NVEASDA---EGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGAT 1047
Cdd:PHA02875    91 GKFADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034640726 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 1034640726  618 AAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHgAEVNKADNeGRTALIAAAYMGHREIVEHLL 697
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81
                           90
                   ....*....|
gi 1034640726  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 1034640726  818 LSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARtnEIDNDGRIPFILASQEGHYDCVQ 897
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1034640726  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 1034640726  582 LTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLyAGVKVDCADaDSRTALRAAAWGGHEDIVL 661
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726  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 1034640726  824 QGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENK 903
Cdd:PHA02876   155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  904 SNIDQRGYDGRNALRVAALEGH------------------------------RDIVELLFSHGADVNCKDADGRPTLYIL 953
Cdd:PHA02876   235 SNINKNDLSLLKAIRNEDLETSlllydagfsvnsiddckntplhhasqapslSRLVPKLLERGADVNAKNIKGETPLYLM 314
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  954 A-----LENQLTMaeyfLENGANVEASDAEGRTALH-VSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKV 1027
Cdd:PHA02876   315 AkngydTENIRTL----IMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1028 VQLLIEHGAVVDHTCNQGATALCIA-AQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNG-HSQIIKLLEKygassl 1105
Cdd:PHA02876   391 INTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLD------ 464
                          330
                   ....*....|....*.
gi 1034640726 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 1034640726  524 REDSIRTLLDNGASVNQCDSNGRTLL---ANAAYSGS--LDVVNLLVSRGADLEIEDAHGHTPLTLAA--RQGHTKVVNC 596
Cdd:PHA03100    47 NIDVVKILLDNGADINSSTKNNSTPLhylSNIKYNLTdvKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEY 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  597 LIGCGANINHTDQDGWTALRSAAWGGH--TEVVSALLYAGVKVDCADAdsrtalraaawgghediVLNLLQHGAEVNKAD 674
Cdd:PHA03100   127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKD 189
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640726  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 1034640726  724 SKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  804 GaaVDSidsegrTVLSIASAqgNVEVVRTLLDRGLDENHRDDAGWTPLHMAafeghrlicealieqgartneIDNdgrip 883
Cdd:PHA02874    91 G--VDT------SILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYA---------------------IKK----- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  884 filasqeghydcvqillenksnidqrgydgrnalrvaaleGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAE 963
Cdd:PHA02874   135 ----------------------------------------GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  964 YFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHvKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA02874   175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID 253
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1034640726 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 1034640726  959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVV 1038
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034640726 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 1034640726  723 ASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEgGADVDHTDnNGRTPLLAAASMGHASVVNTLLF 802
Cdd:pfam12796    5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLE 82

                   ....*....
gi 1034640726  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 1034640726  648 LRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHgAEVNHEDvDGRTALSVAalcvpASKGH 727
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYA-----ARSGH 73
                           90
                   ....*....|....*
gi 1034640726  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 1034640726  549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCgANINHTDqDGWTALRSAAWGGHTEVVS 628
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726  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 1034640726  950 LYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAyHADVNAADNeKRSALQSAAWQGHVKVVQ 1029
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1034640726 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 1034640726  917 LRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENgANVEASDaEGRTALHVSCWQGHMEMVQ 996
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1034640726  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 1034640726  896 VQILLENKSNIDQRGYDGRNALRV---AALEGHRDIVELLFSHGADVNCKDADG-RPTLYILALENQLTMAEYFLENGAN 971
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDVIKLLIKAGAD 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  972 VEASDAEGRTALHVsCWQG---HMEMVQVLIAYHADVNAADNEKRSALQ-----SAAwqgHVKVVQLLIEHGAVVDHTCN 1043
Cdd:PHA03095   110 VNAKDKVGRTPLHV-YLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADVYAVDD 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034640726 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 1034640726 1016 LQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHgADPNHADQfGRTAMRVAAKNGHSQIIK 1095
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                   ....*...
gi 1034640726 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 1034640726  826 NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIpfilaSQEGHYDCVQI---LLEN 902
Cdd:PHA02878    49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAI-----KDAFNNRNVEIfkiILTN 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  903 KSN---------IDQRGYDGrnalrvaALEGhrDIVELLFSHGADVNCKDADGRPTLYILALENQLT-MAEYFLENGANV 972
Cdd:PHA02878   124 RYKniqtidlvyIDKKSKDD-------IIEA--EITKLLLSYGADINMKDRHKGNTALHYATENKDQrLTELLLSYGANV 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  973 EASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAwqGHVK---VVQLLIEHGAVVD-HTCNQGATA 1048
Cdd:PHA02878   195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNaKSYILGLTA 272
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034640726 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 1034640726  963 EYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVD-HT 1041
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDpHA 621
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1042 cnqGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAS-----SLNGCSPSPVHTM 1116
Cdd:PLN03192   622 ---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkanTDDDFSPTELREL 698

                   ...
gi 1034640726 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 1034640726  659 IVLNLLQHGAEVNKADnegrtaliaaaymghreiVEHLLdhgAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRG 738
Cdd:PLN03192   493 ILKNFLQHHKELHDLN------------------VGDLL---GDNGGEHDDPNMASNLLTV---ASTGNAALLEELLKAK 548
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  739 AEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSidSEGRTVL 818
Cdd:PLN03192   549 LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLL 626
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  819 SIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDND------------------G 880
Cdd:PLN03192   627 CTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfsptelrellqkrelgH 706
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  544 NGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGH 623
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  624 TEVVSALLYAGVKV-DCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAE 702
Cdd:PHA02875    81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640726  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 1034640726  645 RTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAALcvpas 724
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE----- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  725 KGHASVVSLLIDRGAEVDHC-DKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW 803
Cdd:PHA02875    78 EGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640726  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 1034640726  730 VVSLLIDRGAEVDHCDKDGMTPLL-----VAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFW- 803
Cdd:PHA02798    53 IVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMi 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  804 --GAAVDSIDSEGRTVLSIASAQGN---VEVVRTLLDRGLDEN-HRDDAGWTPLH-MAAFEGHRL---ICEALIEQGART 873
Cdd:PHA02798   133 enGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLHcYFKYNIDRIdadILKLFVDNGFII 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  874 NEIDNDGRIPFIlasqeghyDCVQILLENKSNIDqrgydgrnalrvaaleghRDIVELLFSHgADVNCKDADGRPTLYIL 953
Cdd:PHA02798   213 NKENKSHKKKFM--------EYLNSLLYDNKRFK------------------KNILDFIFSY-IDINQVDELGFNPLYYS 265
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAA----RQGHTKVVNCLIGCgaNINHTDQdgwtALRSAAWGGHT 624
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKC--SVFYTLV----AIKDAFNNRNV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  625 EVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKAD-NEGRTALIAAAYMGHREIVEHLLDHGAEV 703
Cdd:PHA02878   115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANV 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  704 NHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVA-AYEGHVDVVDLLLEGGADVDHTDN-NG 781
Cdd:PHA02878   195 NIPDKTNNSPLHHAV-----KHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLG 269
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1034640726  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 1034640726  526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRgADLEIEDaHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:pfam12796   11 ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88

                   ...
gi 1034640726  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 1034640726  815 RTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYD 894
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  895 CVQILLENKSNIDQRGY-DGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRptlyilalenqltmaeyflenganve 973
Cdd:PHA02875    83 AVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-------------------------- 136
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  974 asdaegrTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQG-ATALCIA 1052
Cdd:PHA02875   137 -------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYA 209
                          250       260
                   ....*....|....*....|
gi 1034640726 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 1034640726  915 NALRVAALeGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEM 994
Cdd:PLN03192   528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  995 VQVLiaYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHA 1074
Cdd:PLN03192   607 FRIL--YHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
                          170       180
                   ....*....|....*....|....*.
gi 1034640726 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 1034640726  495 EVLQLLVKAGAHVNSEDDRTSCIVRQALERE----DSIRTLLDNGASVNQCDSNGRTLLANAAYSGS--LDVVNLLVSRG 568
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnsySIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  569 ADLEIE----------------DAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLY 632
Cdd:PHA03100   167 VDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                   ..
gi 1034640726  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 1034640726  851 LHMAAFEGHRLICEALIEQgaRTNEID---NDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRD 927
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKN--KGNCINisvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  928 IVELLFSHGADVNckdadgrpTLYILALENQltMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNA 1007
Cdd:PHA02874    83 IIKLLIDNGVDTS--------ILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1008 ADNekrsalqsaawqghvkvvqlliehgavvdhtcnQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAK 1087
Cdd:PHA02874   153 EDD---------------------------------NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  495 EVLQLLVKAGAHVNSEDdrtscivrqaleredSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIE 574
Cdd:PHA03100   157 KILKLLIDKGVDINAKN---------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  751 PLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAA-------------ASMGHASVVNTLLFWGAAVDSIDSEGRTV 817
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  818 LSIASAQGN------------------VEVVRTLLDRGLDENHRD-DAGWTPLHMAAFEGHRLICEALIEQGARTNEIDN 878
Cdd:PHA02878   120 ILTNRYKNIqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  879 DGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNALRVAALE-GHRDIVELLFSHGADVNCKDadgrptlYILALen 957
Cdd:PHA02878   200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-------YILGL-- 270
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  526 DSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANIN 605
Cdd:PHA02875    16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  606 HT-DQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAA 684
Cdd:PHA02875    96 DVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034640726  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 1034640726  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 1034640726  495 EVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLANAAYSGS---LDVVNLLVsR 567
Cdd:PHA03095   168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkpRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLLI-A 246
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034640726  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 1034640726  864 EALIEQGARTNEIdndgriPFILASQEGHYDCVQILLENKS-NIDQRGYDGRNALRVAALEGHRDIVELLfshgadvnck 942
Cdd:cd22192      7 ELHLLQQKRISES------PLLLAAKENDVQAIKKLLKCPScDLFQRGALGETALHVAALYDNLEAAVVL---------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  943 dADGRPTLYILALENQLtmaeYflenganveasdaEGRTALHVSCWQGHMEMVQVLIAYHADVNAAdnekRSA------- 1015
Cdd:cd22192     71 -MEAAPELVNEPMTSDL----Y-------------QGETALHIAVVNQNLNLVRELIARGADVVSP----RATgtffrpg 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1016 -----------LQSAAWQGHVKVVQLLIEHGA----------VVDH--TCNQGATALC-----IAAQEGHIDvvQVLLEH 1067
Cdd:cd22192    129 pknliyygehpLSFAACVGNEEIVRLLIEHGAdiraqdslgnTVLHilVLQPNKTFACqmydlILSYDKEDD--LQPLDL 206
                          250       260
                   ....*....|....*....|....*.
gi 1034640726 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 1034640726 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 1034640726  497 LQLLVKAG--AHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGAdleIE 574
Cdd:PLN03192   541 LEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  706 EDVDGRTA--LSVAaLCVPASKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRT 783
Cdd:PTZ00322    72 EVIDPVVAhmLTVE-LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
                           90
                   ....*....|....*...
gi 1034640726  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 1034640726  759 GHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRTLLDRGl 838
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLG- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  839 deNHRDDA----GWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGR 914
Cdd:PHA02875    92 --KFADDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  764 VDLLLEGGADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSIDSEGRTVLSIASAQGNVEVVRtLLDRGLDENHR 843
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176

                   ....*..
gi 1034640726  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 1034640726 1028 VQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGASSLNG 1107
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177
                           90       100
                   ....*....|....*....|...
gi 1034640726 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 1034640726  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 1034640726  528 IRTLLDNGASVNQCDSN-GRTLLANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINH 606
Cdd:PHA02878   150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  607 TDQDGWTALrsaawggHTEVVSALLYagvkvdcadadsrtalraaawggheDIVLNLLQHGAEVN-KADNEGRTALIAAa 685
Cdd:PHA02878   230 RDKCGNTPL-------HISVGYCKDY-------------------------DILKLLLEHGVDVNaKSYILGLTALHSS- 276
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1034640726  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 1034640726  889 QEGHYDCVQILLENKSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTLYILALENQLTMAEYFLEN 968
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  969 GANVEASDAEGRTALHvscwqgHMEMVQVLIAYHA--DVNAADNEKRSALQSAAWQGHV-KVVQLLIEHGAVVDHTCNQG 1045
Cdd:PHA02876   234 RSNINKNDLSLLKAIR------NEDLETSLLLYDAgfSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKG 307
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034640726 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 1034640726 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 1034640726  580 TPLTLAARQGHTKVVNCLIGCganiNHTD-----QDGWTALRSAAWGGHTEVVSAL---------------LYAGVkvdc 639
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC----PSCDlfqrgALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE---- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  640 adadsrTALRAAAWGGHEDIVLNLLQHGAEVNKADNEG------RTALIA--------AAYMGHREIVEHLLDHGAEVNH 705
Cdd:cd22192     91 ------TALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRA 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034640726  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 1034640726  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 1034640726  808 DSIDSEGRTVLSIA----SAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP 883
Cdd:PTZ00322    72 EVIDPVVAHMLTVElcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
                           90
                   ....*....|....*..
gi 1034640726  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 1034640726  691 EIVEHLLDHGAEVNHEDVDGRTALSVAALcVPASKGHASVVSLLIDRgaEVDHCDKDGMTpllvAAYEGHVDVVDLLLEG 770
Cdd:PHA02878    51 DVVKSLLTRGHNVNQPDHRDLTPLHIICK-EPNKLGMKEMIRSINKC--SVFYTLVAIKD----AFNNRNVEIFKIILTN 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  771 GADVDHTDNNGRTPLLAAASMGHASVVNTLLFWGAAVDSID-SEGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWT 849
Cdd:PHA02878   124 RYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  850 PLHMAAFEGHRLICEALIEQGARTNEIDNDGRIPF-ILASQEGHYDCVQILLENKSNIDQRGY-DGRNALRVAALEghRD 927
Cdd:PHA02878   204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ER 281
                          250
                   ....*....|....*...
gi 1034640726  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 1034640726  624 TEVVSALLYAGVKVDCADADSRTAL-----RAAAWGGHEDIVLNLLQHGAEVNKADNEGRT---ALIAAAYMGHREIVEH 695
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  696 LLDHGAEVNHEDVDGRTALSVAalcvpASKGHA---SVVSLLIDRGAEVD-HCDKDGMTPLLVAAYEG----HVDVVDLL 767
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVY-----LQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNidriDADILKLF 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  768 LEGGADVDHTDNNGRTPLLaaasmghaSVVNTLLFWGAAVDSidsegrtvlsiasaqgnveVVRTLLDRGLDENHRDDAG 847
Cdd:PHA02798   206 VDNGFIINKENKSHKKKFM--------EYLNSLLYDNKRFKK-------------------NILDFIFSYIDINQVDELG 258
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  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 1034640726  927 DIVELLFSHGADVNCKDADGRPTLYILALE-NQLTMAE-----------------------------------YF----- 965
Cdd:PHA02878    51 DVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEmirsinkcsvfytlvaikdafnnrnveifkiiltnRYkniqt 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  966 -----------------------LENGANVEASDAE-GRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAW 1021
Cdd:PHA02878   131 idlvyidkkskddiieaeitkllLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1022 QGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQE-GHIDVVQVLLEHGADPN-HADQFGRTAMRVAAKNghSQIIKLLEK 1099
Cdd:PHA02878   211 HYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGLTALHSSIKS--ERKLKLLLE 288
                          250
                   ....*....|....*.
gi 1034640726 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 1034640726  783 TPLLAAASMGHASVVNTLLfwgaAVDSID-----SEGRTVLSIASAQGNVEVVRTLLD--RGL-DENHRDD--AGWTPLH 852
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL----KCPSCDlfqrgALGETALHVAALYDNLEAAVVLMEaaPELvNEPMTSDlyQGETALH 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  853 MAAFEGHRLICEALIEQGARTneidndgripfILASQEGHYdcvqiLLENKSNIdqrGYDGRNALRVAALEGHRDIVELL 932
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNL---IYYGEHPLSFAACVGNEEIVRLL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  933 FSHGADVNCKDADGRPTLYILALENQLT----MAEYFLenganveASDAEGR-------------TALHVSCWQGHMEMV 995
Cdd:cd22192    156 IEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLIL-------SYDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMF 228

                   ....
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  592 KVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAwgGHEDIVLN----LLQHG 667
Cdd:PHA02946    53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--GTDDEVIErinlLVQYG 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  668 AEVNKA-DNEGRTALIAAAYMGHReIVEHLLDHGAEVNHEDVDGRTALSVAALcvpASKGHASVVSLLIDRGAEVDHCDK 746
Cdd:PHA02946   131 AKINNSvDEEGCGPLLACTDPSER-VFKKIMSIGFEARIVDKFGKNHIHRHLM---SDNPKASTISWMMKLGISPSKPDH 206
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  927 DIVELLFSHGADVNCKDAD-GRPTLYILA----LENQLTMAEYFLENGANVEASDAEGRTALHvscwqghmemvqvliay 1001
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEySTPLCTILSnikdYKHMLDIVKILIENGADINKKNSDGETPLY----------------- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1002 hadvnaadnekrsALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGH---IDVVQVLLEHGADPN-HADQF 1077
Cdd:PHA02798   115 -------------CLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKE 181
                          170       180
                   ....*....|....*....|....
gi 1034640726 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 1034640726  844 DDAGWTPLHMAAFE-------GHRLICEALIEQGARTNEIDNDGRIPFILASQEGHYDCVQILLENKSNIDQRGYDGRNA 916
Cdd:PTZ00322    72 EVIDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1034640726  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 1034640726  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 1034640726  480 TPVRDSLSTLIPKEQEVLQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLD 559
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  560 VVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDG-WTALRSAAWGGHTEVVSALLYAGvkVD 638
Cdd:PHA02875   150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG--AD 227

                   .
gi 1034640726  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 1034640726  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 1034640726  955 LENQLTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEH 1034
Cdd:PHA02875    11 LFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1035 GAVVDHTC-NQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQIIKLLEKYGAsSLN-----GC 1108
Cdd:PHA02875    91 GKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-CLDiedccGC 169

                   ..
gi 1034640726 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 1034640726  549 LANAAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTLAARQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVS 628
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                   ...
gi 1034640726  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 1034640726  710 GRTALSVAALcvpasKGHASVVSLLIDRGAEV--DHCDKD---GMTPLLVAAYEGHVDVVDLLLEGGADVdhtdNNGRtp 784
Cdd:cd22192     51 GETALHVAAL-----YDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSPR-- 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  785 llAAASMGHASVVNTLLFwgaavdsidseGRTVLSIASAQGNVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLI-C 863
Cdd:cd22192    120 --ATGTFFRPGPKNLIYY-----------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFaC 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  959 LTMAEYFLENGANVEASDAEGRTALHVSCWQGHMEMVQVLIA------------------YHADVNAA--------DNEK 1012
Cdd:PHA02878    50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFkiiltnryKNIQ 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1013 RSAL-----QSAAWQGHVKVVQLLIEHGAVVD-HTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAA 1086
Cdd:PHA02878   130 TIDLvyidkKSKDDIIEAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209
                          170       180       190
                   ....*....|....*....|....*....|
gi 1034640726 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 1034640726  807 VDSIDSEGRTVLSIASAQGNVEVVRTLLdrgLDENHRDDAGWTPLHMAAFEGHRlICEALI---EQGAR-------TNEI 876
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDTLLHAISLEYVD-AVEAILlhlLAAFRksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  877 DND----GRIPFILASQEGHYDCVQILLENKSNIDQRG--------------YDGRNALRVAALEGHRDIVELLFSHGAD 938
Cdd:TIGR00870  121 YTSeftpGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPAD 200
                          170       180
                   ....*....|....*....|....*.
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  885 ILASQEGHYDCVQILL---ENKSNIDQ--------RGYDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADG 946
Cdd:cd22193     37 LLNLNPGTNDTIRILLdiaEKTDNLKRfinaeytdEYYEGQTALHIAIERRQGDIVALLVENGADVHAhakgrffQPKYQ 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  947 RPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGRTALHvscwqghmemvqvliayhADVNAADNEK-RSA 1015
Cdd:cd22193    117 GEGFYfgelplsLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH------------------ALVTVADNTKeNTK 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034640726 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 1034640726 1002 HADVNAADNekrsaLQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTA 1081
Cdd:PLN03192   520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
                           90       100
                   ....*....|....*....|...
gi 1034640726 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 1034640726  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 1034640726  911 YDGRNALRVAALEGHRDIVELLFSHGADVNC-------KDADGRPTLY-------ILALENQLTMAEYFLEN---GANVE 973
Cdd:cd22196     92 YKGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPGFYfgelplsLAACTNQLDIVKFLLENphsPADIS 171
                           90
                   ....*....|.
gi 1034640726  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 1034640726 1210 HNLSFTEQIQQHSlprsRSRQSIVSPSSTTQSLGQSHNSPSSEFEWSQVKPSLKsTKASKGGKSENSAKSGSA------- 1282
Cdd:pfam05474  268 HQTKNLSQDQEHG----RKAHKISYPSSRTEERQLHHGEKSVQKDVSKGSISIQ-TEEKIHGKSQNQVTIHSQdqehghk 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1283 -GKKAKQSNSSQPKVLEYEMTQFdRRGPIAKSGTAAPPKQMPAESQCKIMIPSAQQEIGRSQQQFLIHQQSGEQKKRNG- 1360
Cdd:pfam05474  343 eNKISYQSSSTEERHLNCGEKGI-QKGVSKGSISIQTEEQIHGKSQNQVRIPSQAQEYGHKENKISYQSSSTEERRLNSg 421
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726 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 1034640726  992 MEMVQVLIAYHADVNAADNEKRSALQS-----AAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLL- 1065
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTilsniKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1034640726 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 1034640726  619 AWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLD 698
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
                           90
                   ....*....|....*
gi 1034640726  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 1034640726  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 1034640726 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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  884 FILASQEGHYDCVQILLEN--KSNIDQRGYDGRNALRVAALEG-HRDIVELLFSHgadvNCKDADGRPTLYILALENQ-- 958
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEpkKLNINCPDRLGRSALFVAAIENeNLELTELLLNL----SCRGAVGDTLLHAISLEYVda 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  959 -----LTMAEYFLENGANVEASD------AEGRTALHVSCWQGHMEMVQVLIAYHADVNAA---DNEKRSALQSAAWQGh 1024
Cdd:TIGR00870   97 veailLHLLAAFRKSGPLELANDqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHG- 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640726 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 1034640726  654 GGHEDIVLNLLQHGAEVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVAAlcvPASKGHASVVSL 733
Cdd:PHA02946    49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS---GTDDEVIERINL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  734 LIDRGAEVDH-CDKDGMTPLLvAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA--AASMGHASVVNTLLFWGAAVDSI 810
Cdd:PHA02946   126 LVQYGAKINNsVDEEGCGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlMSDNPKASTISWMMKLGISPSKP 204
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  811 DSEGRTVLSIASAQ--GNVEVVRTLLDrGLDENHRDDAGWTPLHMAAfegHRLICEALIEQGARTNEIDNDGRIPFILAS 888
Cdd:PHA02946   205 DHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLI---KTLSPAHLINKLLSTSNVITDQTVNICIFY 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  889 QEGhyDCVQILlenksNIDQRGYDGRNaLRVAALEGHRDIVELLFSHgaDVNCKDAdgrptLYILALENQLTMAEYFLEN 968
Cdd:PHA02946   281 DRD--DVLEII-----NDKGKQYDSTD-FKMAVEVGSIRCVKYLLDN--DIICEDA-----MYYAVLSEYETMVDYLLFN 345

                   ....*
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  839 DENHRDDAGWTPLHMAAFEGH--RLICEALIEQGARtneiDNDGRIPFILASQEGHYdcvqillenksnidqrgYDGRNA 916
Cdd:cd21882     18 SAYQRGATGKTCLHKAALNLNdgVNEAIMLLLEAAP----DSGNPKELVNAPCTDEF-----------------YQGQTA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  917 LRVAALEGHRDIVELLFSHGADVN---CKDA---DGRPTLY-------ILALENQLTMAEYFLENG---ANVEASDAEGR 980
Cdd:cd21882     77 LHIAIENRNLNLVRLLVENGADVSaraTGRFfrkSPGNLFYfgelplsLAACTNQEEIVRLLLENGaqpAALEAQDSLGN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  981 TALHVscwqghmemvQVLIAYhadvNAADNEKRSalqsaawqghVKVVQLLIEHGAVVDHTC-------NQGATALCIAA 1053
Cdd:cd21882    157 TVLHA----------LVLQAD----NTPENSAFV----------CQMYNLLLSYGAHLDPTQqleeipnHQGLTPLKLAA 212
                          250
                   ....*....|...
gi 1034640726 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 1034640726  526 DSIRTLLDNGASVNQCDSNGR----TLLAN-AAYSGSLDVVNLLVSRGADLEIEDAHGHTPLTlaarqghtkvvnCLIGC 600
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYStplcTILSNiKDYKHMLDIVKILIENGADINKKNSDGETPLY------------CLLSN 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  601 GAnINhtdqdgwtalrsaawggHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHE---DIVLNLLQHGAEVNKADN-E 676
Cdd:PHA02798   120 GY-IN-----------------NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNkE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  677 GRTALiaAAYMGHR------EIVEHLLDHGAEVNHEDVDGRTAL--SVAALCVPASKGHASVVSLLIdrgAEVDHCDKD- 747
Cdd:PHA02798   182 KYDTL--HCYFKYNidridaDILKLFVDNGFIINKENKSHKKKFmeYLNSLLYDNKRFKKNILDFIF---SYIDINQVDe 256
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726 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 1034640726 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 1034640726 1025 VKVVQLLIEHGAVVDHTCNQGATALCIAAQEGHI-----DVVQVLLEHGADPNHADQFGRTAMRVAA--KNGHSQIIKLL 1097
Cdd:PHA03100    48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127

                   ....*
gi 1034640726 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 1034640726   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 1034640726  830 VRTLLDRGLDENHRDDAGWTPLHMAAFEGHRLICEALIEQGARTNEIDNDGRIP--FILASQEGHYDCVQILLENKSNID 907
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPlyYLSGTDDEVIERINLLVQYGAKIN 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  908 QRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKDADGRPTL--YILALENQLTMAEYFLENGANVEASDAEGRTALHV 985
Cdd:PHA02946   135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  986 SCWQ--GHMEMVQVLIAyHADVNAADNEKRSALQ---SAAWQGHVkVVQLLIEHGAVVDHTCNqgataLCIAAQEGhiDV 1060
Cdd:PHA02946   215 VCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTlliKTLSPAHL-INKLLSTSNVITDQTVN-----ICIFYDRD--DV 285
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034640726 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 1034640726  495 EVLQLLVKAGAHVN--SEDDRTSCI-----VRQALErEDSIRTLLDNGASVNQCDSNGRTLLAN--AAYSGSLDVVNLLV 565
Cdd:PHA02859    67 EILKFLIENGADVNfkTRDNNLSALhhylsFNKNVE-PEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLI 145
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034640726  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 1034640726  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 1034640726   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 1034640726  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 1034640726  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 1034640726   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 1034640726   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 1034640726  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 1034640726  584 LAArQGHTKVVNCLIGCGANINHTDQDGWTALRSAAWGGHTEVVSALLYAGVKVDCADADSRTALRAAAWGGHEDIVLNL 663
Cdd:PTZ00322    89 LAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
                           90
                   ....*....|.
gi 1034640726  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 1034640726  497 LQLLVKAGAHVNSEDDRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGRTLLANA-AYSGSLDVVNLLVSRGADLEIED 575
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKD 285
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  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 1034640726  710 GRTALSVAALcvpasKGHASVVSLLIDRGAEVD-------------HCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd21882     73 GQTALHIAIE-----NRNLNLVRLLVENGADVSaratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaa 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDSIDS-------EGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd21882    148 LEAQDSLGNTVLHALVLQADNTPENSafvcqmynlLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRE 227
                          170       180
                   ....*....|....*....|....*.
gi 1034640726  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 1034640726  691 EIVEHLL----DHG-------AEVNHEDVDGRTALSVAAlcvpaSKGHASVVSLLIDRGAEVDHCDKD------------ 747
Cdd:cd22194    111 EIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAI-----ERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegf 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  748 --GMTPLLVAAYEGHVDVVDLLLEggadvdhtdnNGRTPLLAAASMGhasvvNTLLFwgAAVD-SIDSEGRTVLSIasaQ 824
Cdd:cd22194    186 yfGETPLALAACTNQPEIVQLLME----------KESTDITSQDSRG-----NTVLH--ALVTvAEDSKTQNDFVK---R 245
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  658 DIVLNLLQHGAEVN-KADNEGRTALiaAAYMGHR-----EIVEHLLDHGAEVNHEDVDGRTALSVaALCVPASKghASVV 731
Cdd:PHA02859    67 EILKFLIENGADVNfKTRDNNLSAL--HHYLSFNknvepEILKILIDSGSSITEEDEDGKNLLHM-YMCNFNVR--INVI 141
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  492 KEQEVLQLLVKAGAHVNSED-DRTSCIV----RQALEREDSIRTLLDNGASVNQC-DSNGRTLLAN--AAYSGSLDVVNL 563
Cdd:PHA02989    86 KIKKIVKLLLKFGADINLKTfNGVSPIVcfiyNSNINNCDMLRFLLSKGINVNDVkNSRGYNLLHMylESFSVKKDVIKI 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  564 LVSRGAD-LEIEDAHGHTPLTLAARQG----HTKVVNCLIGCGANINHTDQdgwtalrsaawgGHTEVVSALLyagvkvd 638
Cdd:PHA02989   166 LLSFGVNlFEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNN------------GSESVLESFL------- 226
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034640726  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 1034640726  885 ILASQEGHYDCVQILLEnksnIDQRG---------------YDGRNALRVAALEGHRDIVELLFSHGADVNCKDAD---- 945
Cdd:cd22197     55 VLNLQDGVNACIMPLLE----IDKDSgnpkplvnaqctdeyYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffq 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  946 ---------GRPTLYILALENQLTMAEYFLENG---ANVEASDAEGRTALhvscwqghmemvqvliayHADVNAADN-EK 1012
Cdd:cd22197    131 kkqgtcfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVL------------------HALVMIADNsPE 192
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034640726 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 1034640726  499 LLVKAGAHVNSEDDRTSCIVRQAL--EREDSIRTLLDNGASVNQCDSNGRTLLANAAYSGSLDVVNLLVSRGADLEIEDA 576
Cdd:PHA03100   177 YLLSYGVPINIKDVYGFTPLHYAVynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256

                   .
gi 1034640726  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 1034640726   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 1034640726  959 LTMAEyflENG-------ANVEASDAEGRTALHVSCWQGHMEMVQVLIAYHADVNAAD-----NEK---------RSALQ 1017
Cdd:cd22194    117 LAFAE---ENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffNPKykhegfyfgETPLA 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726 1018 SAAWQGHVKVVQLLIEH----GAVVDHTCNQGATALCIAAQ--EGHIDVV-----QVLLEHG-----ADPNHAdqfGRTA 1081
Cdd:cd22194    194 LAACTNQPEIVQLLMEKestdITSQDSRGNTVLHALVTVAEdsKTQNDFVkrmydMILLKSEnknleTIRNNE---GLTP 270
                          170
                   ....*....|....
gi 1034640726 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 1034640726  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 1034640726  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 1034640726  720 CVPASKGHASVVSLLIDRGAEVDHCDKD-GMTPL---LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPL---LAAASMg 792
Cdd:PHA02859    58 CLEKDKVNVEILKFLIENGADVNFKTRDnNLSALhhyLSFNKNVEPEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV- 136
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  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 1034640726  908 QRGYDGRNALRVAAL---EGHRDIVELLFshgadvnckDADgRPTLYILALENQLTMAEYFlenganveasdaEGRTALH 984
Cdd:cd21882     21 QRGATGKTCLHKAALnlnDGVNEAIMLLL---------EAA-PDSGNPKELVNAPCTDEFY------------QGQTALH 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  985 VSCWQGHMEMVQVLIAYHADVNAADNekrsalqSAAWQGHvkvvqlliehgavvDHTCNQ-GATALCIAAQEGHIDVVQV 1063
Cdd:cd21882     79 IAIENRNLNLVRLLVENGADVSARAT-------GRFFRKS--------------PGNLFYfGELPLSLAACTNQEEIVRL 137
                          170       180
                   ....*....|....*....|....
gi 1034640726 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 1034640726  481 PVRDSLSTL----IPKEQEVLQLLVKAGAHVNSED--DRTSCIVRQALEREDSIRTLLDNGASVNQCDSNGR-TLLANAA 553
Cdd:PHA02875   131 PNTDKFSPLhlavMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAI 210
                           90       100
                   ....*....|....*....|
gi 1034640726  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 1034640726  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 1034640726  826 NVEVVRTLLDRGLDENHR-DDAGWTPLHmaafegHRL---------ICEALIEQGARTNEIDNDGRIPF--ILASQEGHY 893
Cdd:PHA02859    65 NVEILKFLIENGADVNFKtRDNNLSALH------HYLsfnknvepeILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRI 138
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034640726  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 1034640726  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 1034640726   22 QFYCREWVFHKLQHCLQeksnccnsAVNAPSLVMnsgnnasgvsgkgaawgVLLVGGPGSGKTALCTELLwpsspaslqR 101
Cdd:pfam13191    1 RLVGREEELEQLLDALD--------RVRSGRPPS-----------------VLLTGEAGTGKTTLLRELL---------R 46
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  102 GLHRQALAFHFCKAQD-------SDTLCVGGFIRGLVAQIcRSGLLQGYEDKLRDPAVQSLLQPGECERNPAEAFKRCVL 174
Cdd:pfam13191   47 ALERDGGYFLRGKCDEnlpysplLEALTREGLLRQLLDEL-ESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLD 125
                          170       180
                   ....*....|....*....|.
gi 1034640726  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 1034640726 1026 KVVQLLIEHGAVVDHTCNQGATALCIAAQEGHIDVVQVLLEHGADPNHADQFGRTAMRVAAKNGHSQI--IKLLEKYGAS 1103
Cdd:PHA02946    53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAK 132
                           90
                   ....*....|..
gi 1034640726 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 1034640726  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 1034640726  710 GRTALSVAALCVpaSKGHASVVSLLIDRGAEVDHCDKDGMTPLLVAAYEGH-----------VDVVDLLLEGGADVdHTD 778
Cdd:cd21882     26 GKTCLHKAALNL--NDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQGQtalhiaienrnLNLVRLLVENGADV-SAR 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  779 NNGRT--------------PLLAAASMGHASVVNTLLFWG---AAVDSIDSEGRTVLSIASAQGNVEVVRTLL------- 834
Cdd:cd21882    103 ATGRFfrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVLQADNTPENSAFvcqmynl 182
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  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 1034640726  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 1034640726  545 GRTLLANAAYSGSLDVVNLLVSRGADLEIEDA--------------HGHTPLTLAARQGHTKVVNCLIGCGANINHTDQD 610
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                   ....*
gi 1034640726  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 1034640726  492 KEQEVLQLLVKAGAHVNSEDDRTSCIVRQALE--REDSIRTLLDNGASVNQCDSNGRTLL-------------------- 549
Cdd:PHA02878   179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhyNKPIVHILLENGASTDARDKCGNTPLhisvgyckdydilklllehg 258
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034640726  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 1034640726 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 1034640726  992 MEMVQVLIAYHADVNAADNEKRSALQSAAWQGHVKVVQLLIEHGAVVDHTCNQGATALCIAAQEG--------HIDVVQV 1063
Cdd:PHA02795   201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1034640726 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 1034640726  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 1034640726  708 VDGRTALSVAALCVPASKghasvvsllidrgaEVDHCDKDGMTPLLVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLA 787
Cdd:PHA02795   195 VDEPTVLEIYKLCIPYIE--------------DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDV 260
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1034640726  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 1034640726  493 EQEVLQLLVKAGAHVNSEDDRTSCIVRQALE----REDSIRTLLDNGASVNQCDSNGRTLLAN-AAYSGSLDVVNLLVSR 567
Cdd:PHA02859   102 EPEILKILIDSGSSITEEDEDGKNLLHMYMCnfnvRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSL 181
                           90
                   ....*....|....*..
gi 1034640726  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 1034640726  682 IAAAYMGHR----EIVEHLLDHGAEVNHEDVDGRTALSVAALCVPASkghASVVSLLIDRGAEVDHCDKDGMTPLLvaAY 757
Cdd:PHA02716   180 ILHAYLGNMyvdiDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVC---ASVIKKIIELGGDMDMKCVNGMSPIM--TY 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  758 EGHVDVVDLLLEgGADVDHTDNNGRT--PLLAAASMGHA-----SVVNTLLFWGAAVDSIDSEGRTVLS--IASAQGNVE 828
Cdd:PHA02716   255 IINIDNINPEIT-NIYIESLDGNKVKniPMILHSYITLArnidiSVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTD 333
                          170       180
                   ....*....|....*....|....
gi 1034640726  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 1034640726  669 EVNKADNEGRTALIAAAYMGHREIVEHLLDHGAEVNHEDVDGRTALSVA---ALCVPASKGHASVVSLLIDRGAEVDhCD 745
Cdd:PHA02795   213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAvdrGSVIARRETHLKILEILLREPLSID-CI 291
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1034640726  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 1034640726  927 DIVELLFSHGADVNCKDADGRPTL---YILALEN-QLTMAEYFLENGANVEASDAEGRTALHV--SCWQGHMEMVQVLIA 1000
Cdd:PHA02859    67 EILKFLIENGADVNFKTRDNNLSAlhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLID 146
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1034640726 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 1034640726   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 1034640726  710 GRTALSVAAlcvpaSKGHASVVSLLIDRGAEV-------------DHCDKDGMTPLLVAAYEGHVDVVDLLLEGGAD--- 773
Cdd:cd22197     94 GHSALHIAI-----EKRSLQCVKLLVENGADVharacgrffqkkqGTCFYFGELPLSLAACTKQWDVVNYLLENPHQpas 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  774 VDHTDNNGRTPLLAAASMGHASVVNT---------LLFWGAAVDS-------IDSEGRTVLSIASAQGNVEVVRTLLDRG 837
Cdd:cd22197    169 LQAQDSLGNTVLHALVMIADNSPENSalvikmydgLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQRE 248

                   ....*.
gi 1034640726  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 1034640726  865 ALIEQGARTNEIdndgrIPFILASQEGHyDCVQILLEnkSNIDQRGYDGRNALRVAALEGHRDIVELLFSHGADVNCKdA 944
Cdd:cd22194    101 ALLNINENTKEI-----VRILLAFAEEN-GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH-A 171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  945 DGR---PT------------LYILALENQLTMAEYFLENGANVEAS-DAEGRTALhvscwqghmemvqvliayHADVNAA 1008
Cdd:cd22194    172 KGVffnPKykhegfyfgetpLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVL------------------HALVTVA 233
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034640726 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 1034640726  730 VVSLLIDRGAEVDHCDKDGMTPLLVAAYEGHV--DVVDLLLEGGADVDHTDNNGRTPLLAaaSMGHASVVNTLLFwGAAV 807
Cdd:PHA02716   194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPIMT--YIINIDNINPEIT-NIYI 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034640726  808 DSIDSEGRT------VLSIASAQG-NVEVVRTLLDRGLDENHRDDAGWTPLHMAAFEgHRL---ICEALIEQGARTNEID 877
Cdd:PHA02716   271 ESLDGNKVKnipmilHSYITLARNiDISVVYSFLQPGVKLHYKDSAGRTCLHQYILR-HNIstdIIKLLHEYGNDLNEPD 349
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034640726  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 1034640726  894 DCVQILLENKSNIDQRGYDGR---NALRVAALEGH--RDIVELLFSHGADVNCKDADGRPTLYILALE---NQLTMAEYF 965
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIETplcAVLRNREITSNkiKKIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFL 130
                           90       100
                   ....*....|....*....|.
gi 1034640726  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 1034640726  729 SVVSLLIDRGAEVDHCDKDGMTPL--LVAAYEGHVDVVDLLLEGGADVDHTDNNGRTPLLAAASMghASVVNTLlfwgaa 806
Cdd:PHA02716   298 SVVYSFLQPGVKLHYKDSAGRTCLhqYILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSM--LSVVNIL------ 369
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1034640726  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 1034640726  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 1034640726 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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