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Conserved domains on  [gi|281363919|ref|NP_001163233|]
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uncharacterized protein Dmel_CG42672, isoform D [Drosophila melanogaster]

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];
8-274 9.14e-61

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.58  E-value: 9.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    8 ALLQYIDNNDISGLRAILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDV 87
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   88 VQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNVG 167
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  168 DKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASRE 247
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
                         250       260
                  ....*....|....*....|....*..
gi 281363919  248 GFQDIAASLIAAGAYINIQDRGADTPL 274
Cdd:COG0666   263 GAALIVKLLLLALLLLAAALLDLLTLL 289
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
441-972 1.23e-56

KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.


:

Pssm-ID: 462231  Cd Length: 293  Bit Score: 198.76  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   441 YELYSSALADVLSEPTLTTPITVGLYAKWGSGKSFLLNKLRDEMNNFarqwaeppirtsgllfivclhvalligtivgls 520
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   521 twsavvgvsaavgflllaylllaavrycnyqmdmqwaysvqhglekrmtrlrlilqvafchppgpqsdsqakPVRFHFAE 600
Cdd:pfam07693   48 ------------------------------------------------------------------------NEEFIIVY 55
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   601 ANSASPTG-DGAVAHMLAALLDAIESHYGWLATRLYRAFRPKCLKVDVGWRWRRMCCIPIVLIFELALVTvvtgisltva 679
Cdd:pfam07693   56 FNPWSFSGqDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKIGLIFGVAIILALTGLVVAIE---------- 125
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   680 yftfadekekehilvalyviaavmgtlicthlhvlakvfvslftshirvlkravrssesAPLTMLGAEV-AVMTDMVKCL 758
Cdd:pfam07693  126 -----------------------------------------------------------EPMKKLQTEIeELRSDIESTL 146
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   759 DAftnQQSRLVGVIDALDSCDTERILTLLNAVQTLLSSPNrpFVLLISVDPHVIAKAAEANSRRLFtegGIGGHDFLRNL 838
Cdd:pfam07693  147 KD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPN--VVFILAADEEILKKALEANYESGL---EIDGQKYLEKI 218
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   839 VHLPVYLQNSGLRKVQRAQMTAllFKRSGGGDYQTDDGPTLghsvsarrlsnaseiissqeklrgparggggkklrlses 918
Cdd:pfam07693  219 IQVPFTLPPLSLRQLKKFLMLS--FDNSEEGTSSKDRDETL--------------------------------------- 257
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   919 vasstgsnlhrlgqnpqTVLDLSRIVLTDDyFSDVNPRSMRRLMNVIYITVRLL 972
Cdd:pfam07693  258 -----------------RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-434 4.39e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 4.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  152 DIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVN 231
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  232 ALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAV 311
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  312 EKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRN 391
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281363919  392 PKhsqLLYRANKAGETPYNIDSLHQKTILGQVFGARRLNTNED 434
Cdd:COG0666   242 GA---DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1193-1228 2.24e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


:

Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 37.60  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281363919 1193 LPKLAPVLRENAINGRVLKHCDMPDLKSVLGLSFGH 1228
Cdd:cd09487    11 LEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGH 46
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-274 9.14e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.58  E-value: 9.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    8 ALLQYIDNNDISGLRAILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDV 87
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   88 VQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNVG 167
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  168 DKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASRE 247
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
                         250       260
                  ....*....|....*....|....*..
gi 281363919  248 GFQDIAASLIAAGAYINIQDRGADTPL 274
Cdd:COG0666   263 GAALIVKLLLLALLLLAAALLDLLTLL 289
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
441-972 1.23e-56

KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.


Pssm-ID: 462231  Cd Length: 293  Bit Score: 198.76  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   441 YELYSSALADVLSEPTLTTPITVGLYAKWGSGKSFLLNKLRDEMNNFarqwaeppirtsgllfivclhvalligtivgls 520
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   521 twsavvgvsaavgflllaylllaavrycnyqmdmqwaysvqhglekrmtrlrlilqvafchppgpqsdsqakPVRFHFAE 600
Cdd:pfam07693   48 ------------------------------------------------------------------------NEEFIIVY 55
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   601 ANSASPTG-DGAVAHMLAALLDAIESHYGWLATRLYRAFRPKCLKVDVGWRWRRMCCIPIVLIFELALVTvvtgisltva 679
Cdd:pfam07693   56 FNPWSFSGqDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKIGLIFGVAIILALTGLVVAIE---------- 125
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   680 yftfadekekehilvalyviaavmgtlicthlhvlakvfvslftshirvlkravrssesAPLTMLGAEV-AVMTDMVKCL 758
Cdd:pfam07693  126 -----------------------------------------------------------EPMKKLQTEIeELRSDIESTL 146
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   759 DAftnQQSRLVGVIDALDSCDTERILTLLNAVQTLLSSPNrpFVLLISVDPHVIAKAAEANSRRLFtegGIGGHDFLRNL 838
Cdd:pfam07693  147 KD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPN--VVFILAADEEILKKALEANYESGL---EIDGQKYLEKI 218
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   839 VHLPVYLQNSGLRKVQRAQMTAllFKRSGGGDYQTDDGPTLghsvsarrlsnaseiissqeklrgparggggkklrlses 918
Cdd:pfam07693  219 IQVPFTLPPLSLRQLKKFLMLS--FDNSEEGTSSKDRDETL--------------------------------------- 257
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   919 vasstgsnlhrlgqnpqTVLDLSRIVLTDDyFSDVNPRSMRRLMNVIYITVRLL 972
Cdd:pfam07693  258 -----------------RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-434 4.39e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 4.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  152 DIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVN 231
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  232 ALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAV 311
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  312 EKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRN 391
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281363919  392 PKhsqLLYRANKAGETPYNIDSLHQKTILGQVFGARRLNTNED 434
Cdd:COG0666   242 GA---DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
PHA03095 PHA03095
ankyrin-like protein; Provisional
55-330 6.98e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 110.11  E-value: 6.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTAL-LCASRNGH--LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTE-LVRLLLDKGAD 130
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  131 GNAHGNYHLGAL-LWAAG-RGYKDIVELLVQRGAKVNVGDKYGTTALvwAC----RRGNVEIVDTLLKAGANVDTAGMYS 204
Cdd:PHA03095  110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPL--AVllksRNANVELLRLLIDAGADVYAVDDRF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  205 WTPLLVAAAGGHTD--CVSSILEKKPNVNALDKDGMTAL--------CIASregfqdIAASLIAAGAYINIQDRGADTPL 274
Cdd:PHA03095  188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLhsmatgssCKRS------LVLPLLIAGISINARNRYGQTPL 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919  275 IHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLE 330
Cdd:PHA03095  262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
150-403 1.16e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.52  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  150 YKDIVELLVQRGAKVNVGDKYGTTALVWACR-----RGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAG--GHTDCVSS 222
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  223 ILEKKPNVNALDKDGMTALCIASREGFQD--IAASLIAAGAYINIQDRgadtplihavkaghrtvVEALLKKHADVDIqg 300
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINI-- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  301 KDRKtaiytavekghtpivklllatnpdlesatkdGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRAR 380
Cdd:PHA03100  188 KDVY-------------------------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
                         250       260
                  ....*....|....*....|....*...
gi 281363919  381 SKTIVEALLRN-----PKHSQLLYRANK 403
Cdd:PHA03100  237 NKEIFKLLLNNgpsikTIIETLLYFKDK 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-133 2.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    43 LMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHgAEVEHRDMgGWTSLMWAAYRGHTELVR 122
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 281363919   123 LLLDKGADGNA 133
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
274-366 5.30e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 5.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   274 LIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLAtNPDLESATkDGDTPLLRAVRNRNLEIVH 353
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 281363919   354 LLLDRKAKVTASD 366
Cdd:pfam12796   79 LLLEKGADINVKD 91
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
432-486 1.01e-09

Predicted P-loop ATPase, KAP-like [General function prediction only];


Pssm-ID: 443956  Cd Length: 386  Bit Score: 62.24  E-value: 1.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281363919  432 NEDSEGMLGYELYSSALADVLSEPTLTTPITVGLYAKWGSGKSFLLNKLRDEMNN 486
Cdd:COG4928     1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELES 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-227 7.70e-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: 7.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   74 TALLCASRNGHLDVVQLLLDHGAEVEHRDMG-----GWTSLMWAAYRGHTELVRLLLDKGADG------------NAHGN 136
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  137 YHLG--ALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTAL---------VWACrrgnvEIVDTLLKAGANVDTAGMY-- 203
Cdd:cd22192   133 IYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvlqpnkTFAC-----QMYDLILSYDKEDDLQPLDlv 207
                         170       180
                  ....*....|....*....|....*...
gi 281363919  204 ----SWTPLLVAAAGGHTDCVSSILEKK 227
Cdd:cd22192   208 pnnqGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
260-362 1.86e-06

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: 52.32  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  260 GAYINIQDRGADTPLIHAVKAGHRTVVEALLK-KHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDL--ESATKD- 335
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDl 86
                          90       100
                  ....*....|....*....|....*....
gi 281363919  336 --GDTPLLRAVRNRNLEIVHLLLDRKAKV 362
Cdd:cd22192    87 yqGETALHIAVVNQNLNLVRELIARGADV 115
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
105-130 1.17e-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: 1.17e-04
                            10        20
                    ....*....|....*....|....*.
gi 281363919    105 GWTSLMWAAYRGHTELVRLLLDKGAD 130
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
262-373 1.21e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   262 YINIQDRGADTPLIHAVKAG-HRTVVEALLKKHADVDIQgkdrKTAIYTAV--------------EKGHTPIVKLLLATN 326
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVG----DTLLHAISleyvdaveaillhlLAAFRKSGPLELAND 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 281363919   327 PDLESATKDgDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKrGDTCL 373
Cdd:TIGR00870  120 QYTSEFTPG-ITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFV 164
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
75-258 3.35e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    75 ALLCASRNGHLDVVQLLLDHgAEVEHRDMG---------------GWTSLMWAAYRGHTELVRLLLDKGADGNA------ 133
Cdd:TIGR00870   84 TLLHAISLEYVDAVEAILLH-LLAAFRKSGplelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   134 -----------HGNYHLGAllwAAGRGYKDIVELLVQRGAKVNVGDKYGTTALvwacrrgNVEIVDTLLKAGANVDTAGM 202
Cdd:TIGR00870  163 fvksqgvdsfyHGESPLNA---AACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVMENEFKAEYEELSCQM 232
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919   203 YSwtplLVAAAGGHTdCVSSILEKKPNvnaldKDGMTALCIASREGFQDIAASLIA 258
Cdd:TIGR00870  233 YN----FALSLLDKL-RDSKELEVILN-----HQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
335-364 9.49e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 9.49e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 281363919    335 DGDTPLLRAVRNRNLEIVHLLLDRKAKVTA 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1193-1228 2.24e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 37.60  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281363919 1193 LPKLAPVLRENAINGRVLKHCDMPDLKSVLGLSFGH 1228
Cdd:cd09487    11 LEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGH 46
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-274 9.14e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.58  E-value: 9.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    8 ALLQYIDNNDISGLRAILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDV 87
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   88 VQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNVG 167
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  168 DKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASRE 247
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
                         250       260
                  ....*....|....*....|....*..
gi 281363919  248 GFQDIAASLIAAGAYINIQDRGADTPL 274
Cdd:COG0666   263 GAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-307 1.15e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.11  E-value: 1.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   21 LRAILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEH 100
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  101 RDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACR 180
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  181 RGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIAAG 260
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281363919  261 AYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAI 307
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
441-972 1.23e-56

KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases are sporadically distributed across a wide phylogenetic range in bacteria and in animals. Many of the prokaryotic KAP NTPases are encoded in plasmids and tend to undergo disruption to form pseudogenes. A unique feature of all eukaryotic and certain bacterial KAP NTPases is the presence of two or four transmembrane helices inserted into the P-loop NTPase domain. These transmembrane helices anchor KAP NTPases in the membrane such that the P-loop domain is located on the intracellular side.


Pssm-ID: 462231  Cd Length: 293  Bit Score: 198.76  E-value: 1.23e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   441 YELYSSALADVLSEPTLTTPITVGLYAKWGSGKSFLLNKLRDEMNNFarqwaeppirtsgllfivclhvalligtivgls 520
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   521 twsavvgvsaavgflllaylllaavrycnyqmdmqwaysvqhglekrmtrlrlilqvafchppgpqsdsqakPVRFHFAE 600
Cdd:pfam07693   48 ------------------------------------------------------------------------NEEFIIVY 55
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   601 ANSASPTG-DGAVAHMLAALLDAIESHYGWLATRLYRAFRPKCLKVDVGWRWRRMCCIPIVLIFELALVTvvtgisltva 679
Cdd:pfam07693   56 FNPWSFSGqDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKIGLIFGVAIILALTGLVVAIE---------- 125
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   680 yftfadekekehilvalyviaavmgtlicthlhvlakvfvslftshirvlkravrssesAPLTMLGAEV-AVMTDMVKCL 758
Cdd:pfam07693  126 -----------------------------------------------------------EPMKKLQTEIeELRSDIESTL 146
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   759 DAftnQQSRLVGVIDALDSCDTERILTLLNAVQTLLSSPNrpFVLLISVDPHVIAKAAEANSRRLFtegGIGGHDFLRNL 838
Cdd:pfam07693  147 KD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPN--VVFILAADEEILKKALEANYESGL---EIDGQKYLEKI 218
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   839 VHLPVYLQNSGLRKVQRAQMTAllFKRSGGGDYQTDDGPTLghsvsarrlsnaseiissqeklrgparggggkklrlses 918
Cdd:pfam07693  219 IQVPFTLPPLSLRQLKKFLMLS--FDNSEEGTSSKDRDETL--------------------------------------- 257
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   919 vasstgsnlhrlgqnpqTVLDLSRIVLTDDyFSDVNPRSMRRLMNVIYITVRLL 972
Cdd:pfam07693  258 -----------------RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-340 5.59e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 196.71  E-value: 5.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   59 LARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYH 138
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  139 LGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTD 218
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  219 CVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDI 298
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 281363919  299 QGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPL 340
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-241 2.27e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 2.27e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    7 RALLQYIDNNDISGLRAILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLD 86
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   87 VVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNV 166
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363919  167 GDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTAL 241
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
85-371 2.36e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 2.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   85 LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKV 164
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  165 NVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIA 244
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  245 SREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLA 324
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281363919  325 TNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDT 371
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-405 5.24e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.16  E-value: 5.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  119 ELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVD 198
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  199 TAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAV 278
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  279 KAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDR 358
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 281363919  359 KAKVTASDKRGDTCLHIAMRARSKTIVEALLRNPKHSQLLYRANKAG 405
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
152-434 4.39e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 170.91  E-value: 4.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  152 DIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVN 231
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  232 ALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAV 311
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  312 EKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRN 391
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 281363919  392 PKhsqLLYRANKAGETPYNIDSLHQKTILGQVFGARRLNTNED 434
Cdd:COG0666   242 GA---DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-391 1.65e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  184 VEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIAAGAYI 263
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  264 NIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRA 343
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 281363919  344 VRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRN 391
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
55-330 6.98e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 110.11  E-value: 6.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTAL-LCASRNGH--LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTE-LVRLLLDKGAD 130
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  131 GNAHGNYHLGAL-LWAAG-RGYKDIVELLVQRGAKVNVGDKYGTTALvwAC----RRGNVEIVDTLLKAGANVDTAGMYS 204
Cdd:PHA03095  110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPL--AVllksRNANVELLRLLIDAGADVYAVDDRF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  205 WTPLLVAAAGGHTD--CVSSILEKKPNVNALDKDGMTAL--------CIASregfqdIAASLIAAGAYINIQDRGADTPL 274
Cdd:PHA03095  188 RSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLhsmatgssCKRS------LVLPLLIAGISINARNRYGQTPL 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919  275 IHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLE 330
Cdd:PHA03095  262 HYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA02874 PHA02874
ankyrin repeat protein; Provisional
74-441 1.06e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 108.90  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   74 TALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGallwaagrgyKDI 153
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIE----------KDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  154 VELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVdtagmyswtpllvaaagghtdcvssilekkpnvNAL 233
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV---------------------------------NIE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  234 DKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEk 313
Cdd:PHA02874  154 DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  314 gHTPIVKLLLATNPDLESATKDGDTPLLRAVRNR-NLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSK-TIVEALLRN 391
Cdd:PHA02874  233 -HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdPVIKDIIAN 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281363919  392 PkhsqllYRANKAGETPyNIDSLHQKTIL-GQVFGARRLNTNEDSEGMLGY 441
Cdd:PHA02874  312 A------VLIKEADKLK-DSDFLEHIEIKdNKEFSDFIKECNEEIEDMKKT 355
PHA03100 PHA03100
ankyrin repeat protein; Provisional
150-403 1.16e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.52  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  150 YKDIVELLVQRGAKVNVGDKYGTTALVWACR-----RGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAG--GHTDCVSS 222
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  223 ILEKKPNVNALDKDGMTALCIASREGFQD--IAASLIAAGAYINIQDRgadtplihavkaghrtvVEALLKKHADVDIqg 300
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINI-- 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  301 KDRKtaiytavekghtpivklllatnpdlesatkdGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRAR 380
Cdd:PHA03100  188 KDVY-------------------------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
                         250       260
                  ....*....|....*....|....*...
gi 281363919  381 SKTIVEALLRN-----PKHSQLLYRANK 403
Cdd:PHA03100  237 NKEIFKLLLNNgpsikTIIETLLYFKDK 264
PHA02876 PHA02876
ankyrin repeat protein; Provisional
58-389 8.73e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 105.53  E-value: 8.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   58 FLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNy 137
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  138 hlgALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNV-EIVDTLLKAGANVDTAGMYSWTPLLVAAAGGH 216
Cdd:PHA02876  243 ---SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  217 -TDCVSSILEKKPNVNALDKDGMTALCIASR-EGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHA 294
Cdd:PHA02876  320 dTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  295 DVDIQGKDRKTAIYTAVeKGHTPI--VKLLLATNPDLESATKDGDTPLLRAVRNR-NLEIVHLLLDRKAKVTASDKRGDT 371
Cdd:PHA02876  400 DIEALSQKIGTALHFAL-CGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
                         330
                  ....*....|....*...
gi 281363919  372 CLHIAMRARSktIVEALL 389
Cdd:PHA02876  479 PLLIALEYHG--IVNILL 494
PHA02876 PHA02876
ankyrin repeat protein; Provisional
85-391 5.80e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.83  E-value: 5.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   85 LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGAKV 164
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  165 NVGDkygtTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAA-AGGHTDCVSSILEKKPNVNALDKDGMTALCI 243
Cdd:PHA02876  238 NKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  244 ASREGFQ-DIAASLIAAGAYINIQDRGADTPLIHAVKAG-HRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKL 321
Cdd:PHA02876  314 MAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363919  322 LLATNPDLESATKDGDTPLLRAVRNRNLEI-VHLLLDRKAKVTASDKRGDTCLHIAMRARSK-TIVEALLRN 391
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDN 465
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-133 2.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 2.52e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    43 LMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHgAEVEHRDMgGWTSLMWAAYRGHTELVR 122
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 281363919   123 LLLDKGADGNA 133
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-168 5.66e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 5.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    76 LLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKgADGNAhGNYHLGALLWAAGRGYKDIVE 155
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 281363919   156 LLVQRGAKVNVGD 168
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
119-359 2.16e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 96.25  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  119 ELVRLLLDKGADGNAHGNYH---LGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVE-IVDTLLKAG 194
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGktpLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  195 ANVDTAGMYSWTPLLVAAAGG--HTDCVSSILEKKPNVNALDKDGMTALCI------ASRE--------GFQDIAA---- 254
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANVEllrllidaGADVYAVddrf 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  255 -------------------SLIAAGAYINIQDRGADTPLIHAVKAG--HRTVVEALLKKHADVDIQGKDRKTAIYTAVEK 313
Cdd:PHA03095  188 rsllhhhlqsfkprarivrELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVF 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 281363919  314 GHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRK 359
Cdd:PHA03095  268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313
PHA03100 PHA03100
ankyrin repeat protein; Provisional
86-298 5.30e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 94.73  E-value: 5.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   86 DVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHT-----ELVRLLLDKGADGNAHGNYHLGALLWAAGR--GYKDIVELLV 158
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  159 QRGAKVNVGDKYGTTAL--VWACRRGNVEIVDTLLKAGANVDTagmyswtpllvaaagghTDCVSSILEKKPNVNALDKD 236
Cdd:PHA03100  129 DNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINA-----------------KNRVNYLLSYGVPINIKDVY 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363919  237 GMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDI 298
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
274-366 5.30e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 5.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   274 LIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLAtNPDLESATkDGDTPLLRAVRNRNLEIVH 353
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 281363919   354 LLLDRKAKVTASD 366
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
153-391 5.48e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.56  E-value: 5.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  153 IVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILekkpnVNA 232
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  233 LDKDGMTALCIAsregfQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVE 312
Cdd:PHA02874   92 VDTSILPIPCIE-----KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363919  313 KGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMrARSKTIVEALLRN 391
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLINN 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-234 8.41e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 8.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   142 LLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLL-KAGANVDTAGmysWTPLLVAAAGGHTDCV 220
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNLKDNG---RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 281363919   221 SSILEKKPNVNALD 234
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
62-235 8.50e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 8.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   62 GADVQAEDLDNWTALLCASRNGH-----LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYR--GHTELVRLLLDKGADGNAH 134
Cdd:PHA03100   58 GADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  135 GNYHLGALLWAAGRGYKD--IVELLVQRGAKVNV----------------GDKYGTTALVWACRRGNVEIVDTLLKAGAN 196
Cdd:PHA03100  138 NSDGENLLHLYLESNKIDlkILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 281363919  197 VDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDK 235
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
8-296 2.40e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 91.28  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    8 ALLQY-IDNNDISGLRAILDSRhltiDDRDENATTVLMVVAGRGLTAFVREFLArGADVQAEDLDNWTALLCASRNGHLD 86
Cdd:PHA02876  213 SVLECaVDSKNIDTIKAIIDNR----SNINKNDLSLLKAIRNEDLETSLLLYDA-GFSVNSIDDCKNTPLHHASQAPSLS 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   87 -VVQLLLDHGAEVEHRDMGGWTSLMWAAYRGH-TELVRLLLDKGADGNAHGNYHLGALLWAAGRG-YKDIVELLVQRGAK 163
Cdd:PHA02876  288 rLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGAN 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  164 VNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHT-DCVSSILEKKPNVNALDKDGMTALC 242
Cdd:PHA02876  368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLH 447
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281363919  243 IASREGFQ-DIAASLIAAGAYINIQDRGADTPLIHAVkaGHRTVVEALLKKHADV 296
Cdd:PHA02876  448 YACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
208-299 9.21e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 9.21e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   208 LLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIaAGAYINIQDRGaDTPLIHAVKAGHRTVVE 287
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 281363919   288 ALLKKHADVDIQ 299
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
175-267 1.26e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 1.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   175 LVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKkPNVNALDkDGMTALCIASREGFQDIAA 254
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 281363919   255 SLIAAGAYINIQD 267
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
184-390 7.14e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 7.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  184 VEIVDTLLKAGANVDTAGMYSWTPLlvaaaggHTdCVSSILEKKPnvnaldkdgmtalciasregfqDIAASLIAAGAYI 263
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPL-------HL-YLHYSSEKVK----------------------DIVRLLLEAGADV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  264 NIQDRGADTPLI----HAVKAGhrtVVEALLKKHADVDIQGKDRKTA--IYTAVEKGHTPIVKLLLATNPDLESATKDGD 337
Cdd:PHA03095   77 NAPERCGFTPLHlylyNATTLD---VIKLLIKAGADVNAKDKVGRTPlhVYLSGFNINPKVIRLLLRKGADVNALDLYGM 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 281363919  338 TPLLRAVRNRN--LEIVHLLLDRKAKVTASDKRGDTCLHIAM---RARSKtIVEALLR 390
Cdd:PHA03095  154 TPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLqsfKPRAR-IVRELIR 210
PHA03095 PHA03095
ankyrin-like protein; Provisional
55-257 7.40e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 7.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTALLC--ASRNGHLDVVQLLLDHGAEVEHRDMGGWTSL--MWAAYRGHTELVRLLLDKGAD 130
Cdd:PHA03095  135 IRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCD 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  131 G---NAHGNYHLGALlwAAGRGYKDIVEL-LVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWT 206
Cdd:PHA03095  215 PaatDMLGNTPLHSM--ATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 281363919  207 PLLVAAAGGHTDCVSSILEKKPNVNALDKdgmTALCIASREGFQDIAASLI 257
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAALAKNPSAETVAA---TLNTASVAGGDIPSDATRL 340
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
152-349 2.71e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.45  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  152 DIVELLVQRGAKVnvGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVN 231
Cdd:PLN03192  508 NVGDLLGDNGGEH--DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  232 ALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGadTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAV 311
Cdd:PLN03192  586 IRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 281363919  312 EKGHTPIVKLLLATNPDLESATKDGD---TPLLRAVRNRNL 349
Cdd:PLN03192  664 AEDHVDMVRLLIMNGADVDKANTDDDfspTELRELLQKREL 704
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
33-203 7.73e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   33 DDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWA 112
Cdd:PLN03192  519 EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  113 AYRGHTELVRLLLDKGADGNAHGNYHLgaLLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLK 192
Cdd:PLN03192  599 ISAKHHKIFRILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                         170
                  ....*....|.
gi 281363919  193 AGANVDTAGMY 203
Cdd:PLN03192  677 NGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-391 1.01e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   310 AVEKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDrKAKVTASDKrGDTCLHIAMRARSKTIVEALL 389
Cdd:pfam12796    4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                   ..
gi 281363919   390 RN 391
Cdd:pfam12796   82 EK 83
PHA02878 PHA02878
ankyrin repeat protein; Provisional
118-308 8.32e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 8.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  118 TELVRLLLDKGADGNAHGNYHLG-ALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGAN 196
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  197 VDTAGMYSWTPLLVAAAG-GHTDCVSSILEKKPNVNALDK-DGMTALCIASREgfQDIAASLIAAGAYINIQDRGADTPL 274
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPL 304
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 281363919  275 IHAVKA------GHRTVVEALLKKHADVDIQG----KDRKTAIY 308
Cdd:PHA02878  305 SSAVKQylciniGRILISNICLLKRIKPDIKNsegfIDNMDCIT 348
PHA02875 PHA02875
ankyrin repeat protein; Provisional
152-360 8.33e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.33  E-value: 8.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  152 DIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGA--NVDTAGMYSwtPLLVAAAGGHTDCVSSILEKKPN 229
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  230 VN-ALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIY 308
Cdd:PHA02875   94 ADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281363919  309 TAVEKGHTPIVKLLLATNPDLESATKDGDTPLL-RAVRNRNLEIVHLLLDRKA 360
Cdd:PHA02875  174 IAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
9-102 1.93e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919     9 LLQYIDNNDISGLRAILDSRHlTIDDRDENATTVLMVVAGRGLTAFVReFLARGADVQAEDlDNWTALLCASRNGHLDVV 88
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 281363919    89 QLLLDHGAEVEHRD 102
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
55-166 6.30e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 6.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAH 134
Cdd:PHA02875  118 MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYF 197
                          90       100       110
                  ....*....|....*....|....*....|...
gi 281363919  135 G-NYHLGALLWAAGRGYKDIVELLVQRGAKVNV 166
Cdd:PHA02875  198 GkNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
55-265 1.27e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGA----- 129
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfaddv 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  130 ---DGNAhgNYHLGALLWAAgrgykDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWT 206
Cdd:PHA02875   98 fykDGMT--PLHLATILKKL-----DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  207 PLLVAAAGGHTDCVSSILEKKPNVNALDKDG-MTALCIASREGFQDIAASLIAAGAYINI 265
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
83-331 1.62e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.09  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   83 GHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLVQRGA 162
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  163 KVN-VGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTAL 241
Cdd:PHA02875   93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  242 CIASREGFQDIAASLIAAGAYIN-IQDRGADTPLIHAVKAGHRTVVEALLKKHADVDiqgkdrktaIYTAVEKGHTPIVK 320
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILD 243
                         250
                  ....*....|...
gi 281363919  321 LL--LATNPDLES 331
Cdd:PHA02875  244 MIcnMCTNLESEA 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
260-408 1.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  260 GAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATN--------PDLES 331
Cdd:PHA02874   25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpiPCIEK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  332 AT---------------KDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRNPKHSQ 396
Cdd:PHA02874  105 DMiktildcgidvnikdAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                         170
                  ....*....|..
gi 281363919  397 LlyrANKAGETP 408
Cdd:PHA02874  185 V---KDNNGESP 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
215-389 3.73e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 3.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  215 GHTDCVSSILEKKPNVNALDKDGMTALCIASRegFQDIAAS--LIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALL-- 290
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMK--FRDSEAIklLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdl 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  291 KKHADvDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGD 370
Cdd:PHA02875   91 GKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
                         170
                  ....*....|....*....
gi 281363919  371 TCLHIAMRARSKTIVEALL 389
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
183-383 4.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  183 NVEIVDTLLKAGANVDTAGMYSWTPLLVAAAG----GHTDCVSSILEKK--------------PNV--------NALDKD 236
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSvfytlvaikdafnnRNVeifkiiltNRYKNI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  237 ---GMTALCIASREGFQD--IAASLIAAGAYINIQDRGAD-TPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTA 310
Cdd:PHA02878  129 qtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHA 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281363919  311 VEKGHTPIVKLLLATNPDLESATKDGDTPLLRAV-RNRNLEIVHLLLDRKAKVTA-SDKRGDTCLHIAMRARSKT 383
Cdd:PHA02878  209 VKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSERKL 283
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-125 6.37e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 6.37e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919    72 NWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLL 125
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
198-413 1.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  198 DTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASRE----GFQDIAASLIA---AGAYINIQDRG- 269
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKcsvFYTLVAIKDAFn 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  270 ------ADTPLIHAVKaGHRTVveallkkhADVDIQGKDRKTAIytavekgHTPIVKLLLATNPDLESATKD-GDTPLLR 342
Cdd:PHA02878  111 nrnveiFKIILTNRYK-NIQTI--------DLVYIDKKSKDDII-------EAEITKLLLSYGADINMKDRHkGNTALHY 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281363919  343 AVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRNPKHSQLLyraNKAGETPYNIDS 413
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR---DKCGNTPLHISV 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
240-408 3.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  240 ALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIV 319
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  320 KLLLATNPDLESAT-KDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLrnpKHSQLL 398
Cdd:PHA02875   85 EELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI---DHKACL 161
                         170
                  ....*....|
gi 281363919  399 YRANKAGETP 408
Cdd:PHA02875  162 DIEDCCGCTP 171
PHA02878 PHA02878
ankyrin repeat protein; Provisional
217-381 3.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 3.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  217 TDCVSSILEKKPNVNALDKD-GMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHAD 295
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  296 VDIQGKDRKTAIYTAVEK-GHTPIVKLLLATNPDLES-ATKDGDTPLLRAVRNRnlEIVHLLLDRKAKVTASDKRGDTCL 373
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304

                  ....*...
gi 281363919  374 HIAMRARS 381
Cdd:PHA02878  305 SSAVKQYL 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
182-399 4.72e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  182 GNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKK--PNVNALDKDgmTALCIASREGFQDIAASLIAA 259
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  260 GAYIN-IQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDT 338
Cdd:PHA02875   91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363919  339 PLLRAVRNRNLEIVHLLLDRKAKVTASDKRGD-TCLHIAMRARSKTIVEALLRNPKHSQLLY 399
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
432-486 1.01e-09

Predicted P-loop ATPase, KAP-like [General function prediction only];


Pssm-ID: 443956  Cd Length: 386  Bit Score: 62.24  E-value: 1.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281363919  432 NEDSEGMLGYELYSSALADVLSEPTLTTPITVGLYAKWGSGKSFLLNKLRDEMNN 486
Cdd:COG4928     1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELES 55
PHA02874 PHA02874
ankyrin repeat protein; Provisional
55-295 1.63e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   55 VREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKgadgnah 134
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK------- 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  135 gnyhlgallwaagrgykdivellvqrGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAg 214
Cdd:PHA02874  180 --------------------------GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII- 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  215 gHTDCVSSILEKKPNVNALDKDGMTALCIASREGF-QDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVV------E 287
Cdd:PHA02874  233 -HNRSAIELLINNASINDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikdiiaN 311

                  ....*...
gi 281363919  288 ALLKKHAD 295
Cdd:PHA02874  312 AVLIKEAD 319
PHA02798 PHA02798
ankyrin-like protein; Provisional
85-328 1.81e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.16  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   85 LDVVQLLLDHGAEVEHRDMGGWTSLM-----WAAYRGHTELVRLLLDKGAD---GNAHGNYHLGALLWAAGRGYKDIVEL 156
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADinkKNSDGETPLYCLLSNGYINNLEILLF 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  157 LVQRGAKVNVGDKYGTTALVWACRRGN---VEIVDTLLKAGANVDT-AGMYSWTPLlvaaagghtDCVSsilekKPNVNA 232
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTL---------HCYF-----KYNIDR 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  233 LDKDGM-----TALCI-----ASREGFQDIAASLIAAG------------AYINIQDRGA--DTPLIHAVKAGHRTVVEA 288
Cdd:PHA02798  197 IDADILklfvdNGFIInkenkSHKKKFMEYLNSLLYDNkrfkknildfifSYIDINQVDElgFNPLYYSVSHNNRKIFEY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 281363919  289 LLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPD 328
Cdd:PHA02798  277 LLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
285-391 3.90e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  285 VVEALLKKHADVDIQGKDRKTAIYTAVEKGHTP---IVKLLLATNPDLESATKDGDTPLLRAVRNRN-LEIVHLLLDRKA 360
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108
                          90       100       110
                  ....*....|....*....|....*....|...
gi 281363919  361 KVTASDKRGDTCLHIAMRARS--KTIVEALLRN 391
Cdd:PHA03095  109 DVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRK 141
PHA02798 PHA02798
ankyrin-like protein; Provisional
58-233 7.79e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.85  E-value: 7.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   58 FLARGADVQAEDLDNWTALLCASRNGH---LDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHT---ELVRLLLDKGADG 131
Cdd:PHA02798   95 LIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  132 NAHGNY---------------------------------------------HLGALLWAAGRGYKDIVELLVQRgAKVNV 166
Cdd:PHA02798  175 NTHNNKekydtlhcyfkynidridadilklfvdngfiinkenkshkkkfmeYLNSLLYDNKRFKKNILDFIFSY-IDINQ 253
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363919  167 GDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNAL 233
Cdd:PHA02798  254 VDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTI 320
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-158 2.62e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   105 GWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELLV 158
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
138-191 2.75e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   138 HLGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLL 191
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-356 3.91e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 3.91e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 281363919   305 TAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLL 356
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-257 4.40e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.40e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281363919   205 WTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLI 257
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
283-416 5.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  283 RTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPL-----LRAVRNRNLEIVHLLLD 357
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLE 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281363919  358 RKAKVTASDKRGDTCLHIAM--RARSKTIVEALlrnpkhsqLLYRANKAGETPYNIDSLHQ 416
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYL--------LDNGANVNIKNSDGENLLHL 147
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-227 7.70e-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: 7.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   74 TALLCASRNGHLDVVQLLLDHGAEVEHRDMG-----GWTSLMWAAYRGHTELVRLLLDKGADG------------NAHGN 136
Cdd:cd22192    53 TALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  137 YHLG--ALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTAL---------VWACrrgnvEIVDTLLKAGANVDTAGMY-- 203
Cdd:cd22192   133 IYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilvlqpnkTFAC-----QMYDLILSYDKEDDLQPLDlv 207
                         170       180
                  ....*....|....*....|....*...
gi 281363919  204 ----SWTPLLVAAAGGHTDCVSSILEKK 227
Cdd:cd22192   208 pnnqGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02874 PHA02874
ankyrin repeat protein; Provisional
15-197 2.64e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   15 NNDIsgLRAILDSrHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDH 94
Cdd:PHA02874  103 EKDM--IKTILDC-GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   95 GAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGyKDIVELLVQrGAKVNVGDKYGTTA 174
Cdd:PHA02874  180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLIN-NASINDQDIDGSTP 257
                         170       180
                  ....*....|....*....|....
gi 281363919  175 LVWACRRG-NVEIVDTLLKAGANV 197
Cdd:PHA02874  258 LHHAINPPcDIDIIDILLYHKADI 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-221 2.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.86e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 281363919   171 GTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVAAAGGHTDCVS 221
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
340-429 5.15e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 5.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   340 LLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRNPKhsqllYRANKAGETPynidsLHQKTI 419
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDNGRTA-----LHYAAR 70
                           90
                   ....*....|
gi 281363919   420 LGQVFGARRL 429
Cdd:pfam12796   71 SGHLEIVKLL 80
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
765-1001 1.28e-06

Predicted P-loop ATPase, KAP-like [General function prediction only];


Pssm-ID: 443956  Cd Length: 386  Bit Score: 52.61  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  765 QSRLVGVIDALDSCDTERILTLLNAVQTLLSSPNrpFVLLISVDPHVIAKAAEANSRrlfteGGIGGHDFLRNLVHLPVY 844
Cdd:COG4928   160 GKRLVVFIDDLDRCEPDEAIEVLELIKLFFDFPN--VVFVLAFDREILEHALKERYG-----EDIDAREYLEKIIQVPFR 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  845 LQ--NSGLRKVQRAQMTALLFKRSGGGDYQTDDGPTLGHSVSARRLSNASEIISSQEKLRGPARGGGGKKLRLSESVASS 922
Cdd:COG4928   233 LPplSNELLILELDRLLELLLSALLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLLALLVLLLKLELLLENLLLA 312
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281363919  923 TGSNLHrlgqnpqTVLDLSRIVLTDDYFSDVNPRSMRRLMNVIYITVRLLKAFQIEfsWYRLSSWINLTEQWPLRASMI 1001
Cdd:COG4928   313 ALLLLL-------DELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTL--ELKLEEERELSAKYRLEKRLL 382
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
260-362 1.86e-06

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: 52.32  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  260 GAYINIQDRGADTPLIHAVKAGHRTVVEALLK-KHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDL--ESATKD- 335
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDl 86
                          90       100
                  ....*....|....*....|....*....
gi 281363919  336 --GDTPLLRAVRNRNLEIVHLLLDRKAKV 362
Cdd:cd22192    87 yqGETALHIAVVNQNLNLVRELIARGADV 115
PHA02875 PHA02875
ankyrin repeat protein; Provisional
71-202 4.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   71 DNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGY 150
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 281363919  151 KDIVELLVQRGAKVN-VGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGM 202
Cdd:PHA02875  181 IAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
46-125 5.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   46 VAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLL 125
Cdd:PTZ00322   89 LAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-323 7.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 7.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 281363919   272 TPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLL 323
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
118-361 9.33e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.12  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  118 TELVRLLLDKGADGNAHGNYH--LGALL---WAAGRGYKDIVELLVQRGAKVNVGDKYGTTALV---WACRRGNVEIVDT 189
Cdd:PHA02989   50 IKIVKLLIDNGADVNYKGYIEtpLCAVLrnrEITSNKIKKIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  190 LLKAGANV----DTAG-----MYSWTPLLvaaaggHTDCVSSILEKkpNVNALDKD---GMTALCIASREGFQDIAAS-- 255
Cdd:PHA02989  130 LLSKGINVndvkNSRGynllhMYLESFSV------KKDVIKILLSF--GVNLFEKTslyGLTPMNIYLRNDIDVISIKvi 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  256 --LIAAGAYINIQDRGADTPL---IHAVKAGHR---TVVEALLKKhadVDIQGKDrktaiytavEKGHTPIV-------- 319
Cdd:PHA02989  202 kyLIKKGVNIETNNNGSESVLesfLDNNKILSKkefKVLNFILKY---IKINKKD---------KKGFNPLLisakvdny 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 281363919  320 ---KLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAK 361
Cdd:PHA02989  270 eafNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPG 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-92 1.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281363919    40 TTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLL 92
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
32-175 1.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   32 IDDRDENA-TTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLM 110
Cdd:PHA02878  160 INMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919  111 WA-AYRGHTELVRLLLDKGADGNAHgNYHLGALLWAAGRGYKDIVELLVQRGAKVNVGDKYGTTAL 175
Cdd:PHA02878  240 ISvGYCKDYDILKLLLEHGVDVNAK-SYILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTPL 304
Ank_4 pfam13637
Ankyrin repeats (many copies);
336-389 1.80e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 281363919   336 GDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALL 389
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
71-102 2.07e-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: 42.66  E-value: 2.07e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 281363919    71 DNWTAL-LCASRNGHLDVVQLLLDHGAEVEHRD 102
Cdd:pfam00023    1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
91-142 3.51e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 3.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281363919    91 LLDHG-AEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGAL 142
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
314-390 4.06e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363919  314 GHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLR 390
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
190-256 6.82e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 6.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281363919  190 LLKAGANVDTAGMYSWTPLLVAAAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASL 256
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
156-211 8.51e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 8.51e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919   156 LLVQRGAKVNVGDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYSWTPLLVA 211
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
105-130 1.17e-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: 1.17e-04
                            10        20
                    ....*....|....*....|....*.
gi 281363919    105 GWTSLMWAAYRGHTELVRLLLDKGAD 130
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
262-373 1.21e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   262 YINIQDRGADTPLIHAVKAG-HRTVVEALLKKHADVDIQgkdrKTAIYTAV--------------EKGHTPIVKLLLATN 326
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVG----DTLLHAISleyvdaveaillhlLAAFRKSGPLELAND 119
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 281363919   327 PDLESATKDgDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKrGDTCL 373
Cdd:TIGR00870  120 QYTSEFTPG-ITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFV 164
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
274-356 1.23e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  274 LIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNRNLEIVH 353
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 281363919  354 LLL 356
Cdd:PTZ00322  166 LLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
58-130 1.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 1.38e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281363919   58 FLARGADVQAEDLDNWTALLCASRNGHLDVVQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGAD 130
Cdd:PHA03100  178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
71-99 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
                    ....*....|....*....|....*....
gi 281363919     71 DNWTALLCASRNGHLDVVQLLLDHGAEVE 99
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
285-375 1.61e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  285 VVEALLKKHADVDIQGKDRKTAIYTAVE-----KGHTPIVKLLLATNPDLESATKDGDTPLLRAVRNR---NLEIVHLLL 356
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMI 132
                          90
                  ....*....|....*....
gi 281363919  357 DRKAKVTASDKRGDTCLHI 375
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQV 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
105-136 1.81e-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: 39.97  E-value: 1.81e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 281363919   105 GWTSLMWAAYR-GHTELVRLLLDKGADGNAHGN 136
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-307 2.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 2.27e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281363919   256 LIAAG-AYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAI 307
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
71-100 2.29e-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: 2.29e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 281363919    71 DNWTALLCASRNGHLDVVQLLLDHGAEVEH 100
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
75-258 3.35e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    75 ALLCASRNGHLDVVQLLLDHgAEVEHRDMG---------------GWTSLMWAAYRGHTELVRLLLDKGADGNA------ 133
Cdd:TIGR00870   84 TLLHAISLEYVDAVEAILLH-LLAAFRKSGplelandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   134 -----------HGNYHLGAllwAAGRGYKDIVELLVQRGAKVNVGDKYGTTALvwacrrgNVEIVDTLLKAGANVDTAGM 202
Cdd:TIGR00870  163 fvksqgvdsfyHGESPLNA---AACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVMENEFKAEYEELSCQM 232
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919   203 YSwtplLVAAAGGHTdCVSSILEKKPNvnaldKDGMTALCIASREGFQDIAASLIA 258
Cdd:TIGR00870  233 YN----FALSLLDKL-RDSKELEVILN-----HQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
170-198 3.35e-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: 3.35e-04
                            10        20
                    ....*....|....*....|....*....
gi 281363919    170 YGTTALVWACRRGNVEIVDTLLKAGANVD 198
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
76-231 4.23e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   76 LLCASRNGHLDVvqlLLDhgAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGN------------YHLG--A 141
Cdd:cd22194   117 LAFAEENGILDR---FIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegFYFGetP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  142 LLWAAGRGYKDIVELLVQRGAK-VNVGDKYGTT---ALVWACRRGN------VEIVDTLLKAGANVDTAGMYS---WTPL 208
Cdd:cd22194   192 LALAACTNQPEIVQLLMEKESTdITSQDSRGNTvlhALVTVAEDSKtqndfvKRMYDMILLKSENKNLETIRNnegLTPL 271
                         170       180
                  ....*....|....*....|....*..
gi 281363919  209 LVAAAGGHTDCVSSILEK----KPNVN 231
Cdd:cd22194   272 QLAAKMGKAEILKYILSReikeKPNRS 298
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
105-133 4.51e-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: 38.78  E-value: 4.51e-04
                           10        20
                   ....*....|....*....|....*....
gi 281363919   105 GWTSLMWAAYRGHTELVRLLLDKGADGNA 133
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
150-246 4.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  150 YKDIVELLVQRGAKVNV----GDKYGTTALVWACRRGNVEIVDTLLKAGANVDTAGMYS-WTPLLVAAAGGHTDCVSSIL 224
Cdd:PHA02884   45 YTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 281363919  225 EKKPNVNALDKDGMTALCIASR 246
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
212-291 5.97e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  212 AAGGHTDCVSSILEKKPNVNALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLK 291
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
9-97 6.56e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919    9 LLQYIDNNDISGLRAILDSRHLTiDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTALLCASRNGHLDVV 88
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                  ....*....
gi 281363919   89 QLLLDHGAE 97
Cdd:PTZ00322  165 QLLSRHSQC 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
241-323 8.69e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  241 LCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHAVKAGHRTVVEALLKKHADVDIQGKDRKTAIYTAVEKGHTPIVK 320
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 281363919  321 LLL 323
Cdd:PTZ00322  166 LLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
335-364 9.49e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 9.49e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 281363919    335 DGDTPLLRAVRNRNLEIVHLLLDRKAKVTA 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
237-361 1.28e-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: 43.21  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  237 GMTALCIASREGFQDIAASLIAAGAYINIQDRG--------------ADTPLIHAVKAGHRTVVEALLKK-HADVDIQGK 301
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKeSTDITSQDS 220
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281363919  302 DRKTAIYTAVE-----KGHTPIVK------LLLATNPDLESAT-KDGDTPLLRAVRNRNLEIVHLLLDRKAK 361
Cdd:cd22194   221 RGNTVLHALVTvaedsKTQNDFVKrmydmiLLKSENKNLETIRnNEGLTPLQLAAKMGKAEILKYILSREIK 292
PHA02878 PHA02878
ankyrin repeat protein; Provisional
339-420 1.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  339 PLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIAMRARSKTIVEALLRNPKHSQLLYRANKAGETPYNIDSLHQKT 418
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119

                  ..
gi 281363919  419 IL 420
Cdd:PHA02878  120 IL 121
Ank_5 pfam13857
Ankyrin repeats (many copies);
321-376 1.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919   321 LLLATNPDLESATKDGDTPLLRAVRNRNLEIVHLLLDRKAKVTASDKRGDTCLHIA 376
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
304-374 1.88e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919  304 KTAIYTAVEKGHTPIVKLLLATNPDLESATKD--------------GDTPLLRAVRNRNLEIVHLLLD---RKAKVTASD 366
Cdd:cd22193    77 QTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQD 156

                  ....*...
gi 281363919  367 KRGDTCLH 374
Cdd:cd22193   157 SRGNTVLH 164
Ank_5 pfam13857
Ankyrin repeats (many copies);
223-277 1.89e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.89e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 281363919   223 ILEKKP-NVNALDKDGMTALCIASREGFQDIAASLIAAGAYINIQDRGADTPLIHA 277
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
170-198 1.90e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.90e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 281363919   170 YGTTALVWAC-RRGNVEIVDTLLKAGANVD 198
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
293-343 1.98e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.98e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 281363919   293 HADVDIQGKDRKTAIYTAVEKGHTPIVKLLLATNPDLESATKDGDTPLLRA 343
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
1193-1228 2.24e-03

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 37.60  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 281363919 1193 LPKLAPVLRENAINGRVLKHCDMPDLKSVLGLSFGH 1228
Cdd:cd09487    11 LEQYADLFRKNEIDGDALLLLTDEDLKELGITSPGH 46
Ank_5 pfam13857
Ankyrin repeats (many copies);
24-76 2.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281363919    24 ILDSRHLTIDDRDENATTVLMVVAGRGLTAFVREFLARGADVQAEDLDNWTAL 76
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
88-157 3.88e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 3.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281363919   88 VQLLLDHGAEVEHRDMGGWTSLMWAAYRGHTELVRLLLDKGADGNAHGNYHLGALLWAAGRGYKDIVELL 157
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
335-367 4.79e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 4.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 281363919   335 DGDTPLLRAV-RNRNLEIVHLLLDRKAKVTASDK 367
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
271-298 6.39e-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: 6.39e-03
                            10        20
                    ....*....|....*....|....*...
gi 281363919    271 DTPLIHAVKAGHRTVVEALLKKHADVDI 298
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-301 6.50e-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. 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: 35.73  E-value: 6.50e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 281363919   271 DTPLIHAV-KAGHRTVVEALLKKHADVDIQGK 301
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
173-199 6.93e-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: 6.93e-03
                           10        20
                   ....*....|....*....|....*..
gi 281363919   173 TALVWACRRGNVEIVDTLLKAGANVDT 199
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
335-362 8.43e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 8.43e-03
                           10        20
                   ....*....|....*....|....*...
gi 281363919   335 DGDTPLLRAVRNRNLEIVHLLLDRKAKV 362
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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