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Conserved domains on  [gi|1622856719|ref|XP_028687829|]
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kinase D-interacting substrate of 220 kDa isoform X7 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
340-853 1.39e-57

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: 201.07  E-value: 1.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  340 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgglgllfaft 419
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  420 vhpnlgiavslsflallyiffiviyfggrregeswnwawvlstrlarhigylelllklmfvnppelpeqttkalPVRFLF 499
Cdd:pfam07693   48 --------------------------------------------------------------------------NEEFII 53
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  500 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDTQGKKK--WKKTCCLPSFVIFLFIIGciisgitll 577
Cdd:pfam07693   54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  578 aifrvdpkhltvnavlisiasivglafvlncrtwwqvldsllnsqrkrlhnaasklhklksEGFMKVLKCEV-ELMARMA 656
Cdd:pfam07693  125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  657 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 736
Cdd:pfam07693  144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  737 IVHLPVFLNSRGLSNARKFLVTSAtngdvpcsdttgiqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 816
Cdd:pfam07693  218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1622856719  817 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 853
Cdd:pfam07693  258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-272 3.64e-57

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    4 WTALMWACYKGRTDVVDLLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHL 83
Cdd:COG0666     21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   84 ECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 163
Cdd:COG0666    101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  164 IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKAT 243
Cdd:COG0666    181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
                          250       260
                   ....*....|....*....|....*....
gi 1622856719  244 KMRNIEVVELLLDKGAKVSAVDKKGDTPL 272
Cdd:COG0666    261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02736 super family cl31498
Viral ankyrin protein; Provisional
248-312 1.72e-05

Viral ankyrin protein; Provisional


The actual alignment was detected with superfamily member PHA02736:

Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 1.72e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  248 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 312
Cdd:PHA02736    71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
 
Name Accession Description Interval E-value
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
340-853 1.39e-57

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: 201.07  E-value: 1.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  340 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgglgllfaft 419
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  420 vhpnlgiavslsflallyiffiviyfggrregeswnwawvlstrlarhigylelllklmfvnppelpeqttkalPVRFLF 499
Cdd:pfam07693   48 --------------------------------------------------------------------------NEEFII 53
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  500 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDTQGKKK--WKKTCCLPSFVIFLFIIGciisgitll 577
Cdd:pfam07693   54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  578 aifrvdpkhltvnavlisiasivglafvlncrtwwqvldsllnsqrkrlhnaasklhklksEGFMKVLKCEV-ELMARMA 656
Cdd:pfam07693  125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  657 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 736
Cdd:pfam07693  144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  737 IVHLPVFLNSRGLSNARKFLVTSAtngdvpcsdttgiqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 816
Cdd:pfam07693  218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1622856719  817 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 853
Cdd:pfam07693  258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-272 3.64e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    4 WTALMWACYKGRTDVVDLLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHL 83
Cdd:COG0666     21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   84 ECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 163
Cdd:COG0666    101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  164 IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKAT 243
Cdd:COG0666    181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
                          250       260
                   ....*....|....*....|....*....
gi 1622856719  244 KMRNIEVVELLLDKGAKVSAVDKKGDTPL 272
Cdd:COG0666    261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
52-302 8.16e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 8.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   52 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 126
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  127 PNVNLTDKDGNTALMIAS--KEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 202
Cdd:PHA03100    97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  203 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRK 282
Cdd:PHA03100   172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
                          250       260
                   ....*....|....*....|....*
gi 1622856719  283 LAELLLRN-----PKDGRLLYRPNK 302
Cdd:PHA03100   240 IFKLLLNNgpsikTIIETLLYFKDK 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
74-166 4.13e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 4.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   74 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHTEIVQ 153
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1622856719  154 DLLDAGTYVNIPD 166
Cdd:pfam12796   79 LLLEKGADINVKD 91
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
331-887 6.43e-13

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


Pssm-ID: 443956  Cd Length: 386  Bit Score: 71.87  E-value: 6.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  331 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivfltlllcg 410
Cdd:COG4928      1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  411 glgllfaftvhpnlgiavslsflallyifFIVIYFggrregeswnwawvlstrlarhigylelllklmfvNPpelpeqtt 490
Cdd:COG4928     59 -----------------------------VIVVYF-----------------------------------NA-------- 66
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  491 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDTQGKKKWKKtcclpsfviflfiigcI 570
Cdd:COG4928     67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  571 ISGITLLAIfrvdpkhltvnavlisIASIVGLafvlncrtWWQVLDSLLNSQRKRLHNAASK-LHKLKSEgFMKVLKcev 649
Cdd:COG4928    105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  650 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 729
Cdd:COG4928    157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  730 GHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDVPcsdttGIQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQM 809
Cdd:COG4928    219 AREYLEKIIQVPFRLPPLSNELLILELDRLLELLLSA-----LLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLL 293
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622856719  810 QRTITRQMSFDLTKLLVTEDW-FSDISPQTMRRLLNIVSVTGRLLRANQISFNWDRLASWINLTEQWPYRTSWLILYLE 887
Cdd:COG4928    294 ALLVLLLKLELLLENLLLAALlLLLDELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTLELKLEEERELS 372
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
103-310 1.25e-11

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: 68.89  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  103 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHTEIVQDLLDAG-TYVNIPDRS----GDTVLIG 175
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  176 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 246
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622856719  247 NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 310
Cdd:cd22192    148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
77-322 2.02e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.01  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   77 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHtEIVQD 154
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  155 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 220
Cdd:TIGR00870  100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  221 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-----RGRSRKLA----ELLLR-- 289
Cdd:TIGR00870  168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELScqmyNFALSll 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622856719  290 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 322
Cdd:TIGR00870  241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
3-31 1.61e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.61e-05
                            10        20
                    ....*....|....*....|....*....
gi 1622856719     3 GWTALMWACYKGRTDVVDLLLSHGANPSV 31
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
248-312 1.72e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 1.72e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  248 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 312
Cdd:PHA02736    71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
 
Name Accession Description Interval E-value
KAP_NTPase pfam07693
KAP family P-loop domain; The KAP (after Kidins220/ARMS and PifA) family of predicted NTPases ...
340-853 1.39e-57

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: 201.07  E-value: 1.39e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  340 YDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFagqqieplfqfswlivfltlllcgglgllfaft 419
Cdd:pfam07693    1 RDPYAENLAKLLVDSSPAPGLVIGLYGQWGSGKTSFLNLLEKELNEF--------------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  420 vhpnlgiavslsflallyiffiviyfggrregeswnwawvlstrlarhigylelllklmfvnppelpeqttkalPVRFLF 499
Cdd:pfam07693   48 --------------------------------------------------------------------------NEEFII 53
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  500 TDYNRLSSVGGETSLAEMIATLSDACEREFGFLATRLFRVFKTEDTQGKKK--WKKTCCLPSFVIFLFIIGciisgitll 577
Cdd:pfam07693   54 VYFNPWSFSGQDDLDAELFSALADALEEEYSQLATKLLIGKKLPALGIDAKigLIFGVAIILALTGLVVAI--------- 124
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  578 aifrvdpkhltvnavlisiasivglafvlncrtwwqvldsllnsqrkrlhnaasklhklksEGFMKVLKCEV-ELMARMA 656
Cdd:pfam07693  125 -------------------------------------------------------------EEPMKKLQTEIeELRSDIE 143
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  657 KTIDSftqNQTRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNSVLrdsNINGHDYMRN 736
Cdd:pfam07693  144 STLKD---LNKRIVIIIDDLDRCEPEEIVLLLEAVRLLFDFPNVVFILAADEEILKKALEANYESGL---EIDGQKYLEK 217
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  737 IVHLPVFLNSRGLSNARKFLVTSAtngdvpcsdttgiqedadrrvsQNSLGEMTKLGSKTALnrrdtyrrrqmqrtitrq 816
Cdd:pfam07693  218 IIQVPFTLPPLSLRQLKKFLMLSF----------------------DNSEEGTSSKDRDETL------------------ 257
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1622856719  817 MSFDLTKLLVTEDwFSDISPQTMRRLLNIVSVTGRLL 853
Cdd:pfam07693  258 RALRLNIILLSED-KSNINPRLLKRLINALSITYRLL 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-272 3.64e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.80  E-value: 3.64e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    4 WTALMWACYKGRTDVVDLLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHL 83
Cdd:COG0666     21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   84 ECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVN 163
Cdd:COG0666    101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  164 IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKAT 243
Cdd:COG0666    181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
                          250       260
                   ....*....|....*....|....*....
gi 1622856719  244 KMRNIEVVELLLDKGAKVSAVDKKGDTPL 272
Cdd:COG0666    261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-293 1.88e-55

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 194.79  E-value: 1.88e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   21 LLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEG 100
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  101 ANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGG 180
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  181 HVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAK 260
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622856719  261 VSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKD 293
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-206 1.64e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 189.01  E-value: 1.64e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    1 MGGWTALMWACYKGRTDVVDLLLSHGANPSVTGlQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARK 80
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   81 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGT 160
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1622856719  161 YVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 206
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-314 6.42e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 187.47  E-value: 6.42e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   50 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV 129
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  130 NLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWA 209
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  210 VEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLr 289
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL- 239
                          250       260
                   ....*....|....*....|....*
gi 1622856719  290 npKDGRLLYRPNKAGETPYNIDCSH 314
Cdd:COG0666    240 --EAGADLNAKDKDGLTALLLAAAA 262
PHA03100 PHA03100
ankyrin repeat protein; Provisional
52-302 8.16e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 8.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   52 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQS-VKEI----LKRN 126
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdVKEIvkllLEYG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  127 PNVNLTDKDGNTALMIAS--KEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV--EIVRALLQKYADIDIrgqdn 202
Cdd:PHA03100    97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA----- 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  203 KTALYWAVEKGNATMVRDILqcnpdteictkdGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRK 282
Cdd:PHA03100   172 KNRVNYLLSYGVPINIKDVY------------GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
                          250       260
                   ....*....|....*....|....*
gi 1622856719  283 LAELLLRN-----PKDGRLLYRPNK 302
Cdd:PHA03100   240 IFKLLLNNgpsikTIIETLLYFKDK 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
74-166 4.13e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 4.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   74 LVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKrNPNVNLTDkDGNTALMIASKEGHTEIVQ 153
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1622856719  154 DLLDAGTYVNIPD 166
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
5-277 5.34e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 5.34e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    5 TALMWACYKGRTDVVDLLLSHGANpsVTGLQYSV-YPIIWAAGRGHADIVHLLLQNGAK-----VNCSDKygttplvwaa 78
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGAD--INHINTKIpHPLLTAIKIGAHDIIKLLIDNGVDtsilpIPCIEK---------- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   79 rkghlECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDA 158
Cdd:PHA02874   105 -----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  159 GTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMvrDILQCNPDTEICTKDGETP 238
Cdd:PHA02874   180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTP 257
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1622856719  239 LIKATKMR-NIEVVELLLDKGAKVSAVDKKGDTPLHIAIR 277
Cdd:PHA02874   258 LHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
12-310 1.19e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 99.27  E-value: 1.19e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   12 YKGRTDVVDLLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA 91
Cdd:PHA02874    10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   92 MGADVDqegansmtalIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDT 171
Cdd:PHA02874    90 NGVDTS----------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  172 VLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATkMRNIEVV 251
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAI 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  252 ELLLDKgAKVSAVDKKGDTPLHIAIRGR-SRKLAELLLRNPKDgrLLYRPNKaGETPYNI 310
Cdd:PHA02874   239 ELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKAD--ISIKDNK-GENPIDT 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
5-299 3.78e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 99.75  E-value: 3.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    5 TALMWACYKGRTDVVDLLLSHGANPSV------TGLQYSV----------------------YPIIWAAGRGHADIVHLL 56
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIialddlSVLECAVdsknidtikaiidnrsninkndLSLLKAIRNEDLETSLLL 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   57 LQNGAKVNCSDKYGTTPLVWAARKGHL-ECVKHLLAMGADVDQEGANSMTALIVAVKGGY-TQSVKEILKRNPNVNLTDK 134
Cdd:PHA02876   260 YDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  135 DGNTALMIASK-EGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKG 213
Cdd:PHA02876   340 LYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT 419
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  214 NATM-VRDILQCNPDTEICTKDGETPLIKATKMR-NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSrkLAELLLR-- 289
Cdd:PHA02876   420 NPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHyg 497
                          330
                   ....*....|.
gi 1622856719  290 -NPKDGRLLYR 299
Cdd:PHA02876   498 aELRDSRVLHK 508
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-98 6.54e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 6.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    7 LMWACYKGRTDVVDLLLSHGANPSVTgLQYSVYPIIWAAGRGHADIVHLLLQNgAKVNCSDkYGTTPLVWAARKGHLECV 86
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|..
gi 1622856719   87 KHLLAMGADVDQ 98
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-133 8.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   41 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLA-MGADVDQEGansMTALIVAVKGGYTQSV 119
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNG---RTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1622856719  120 KEILKRNPNVNLTD 133
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
107-198 3.13e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 3.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  107 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTyVNIPDrSGDTVLIGAVRGGHVEIVR 186
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 1622856719  187 ALLQKYADIDIR 198
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
173-265 5.01e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 5.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  173 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRdILQCNPDTEICTkDGETPLIKATKMRNIEVVE 252
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1622856719  253 LLLDKGAKVSAVD 265
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
52-275 5.09e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 92.82  E-value: 5.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   52 IVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNL 131
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  132 TDkdgnTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHV-EIVRALLQKYADIDIRGQDNKTALYWAV 210
Cdd:PHA02876   240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMA 315
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622856719  211 EKGNATM-VRDILQCNPDTEICTKDGETPLIKATKM-RNIEVVELLLDKGAKVSAVDKKGDTPLHIA 275
Cdd:PHA02876   316 KNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYA 382
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-234 1.30e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  140 LMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLqKYADIDIRGqDNKTALYWAVEKGNATMVR 219
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|....*
gi 1622856719  220 DILQCNPDteICTKD 234
Cdd:pfam12796   79 LLLEKGAD--INVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
81-298 2.16e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 2.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   81 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRN--PNVNLTDKDgnTALMIASKEGHTEIVQDLLDA 158
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDVKYPDIE--SELHDAVEEGDVKAVEELLDL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  159 GTYVN-IPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGET 237
Cdd:PHA02875    91 GKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622856719  238 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGD-TPLHIAIRGRSRKLAELLLRNPKDGRLLY 298
Cdd:PHA02875   171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
119-289 3.73e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.93  E-value: 3.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  119 VKEILKRNPNVNLTDKDGNTAL---MIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVE-IVRALLQKYAD 194
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  195 IDIRGQDNKTAL--YWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVDKKGDT 270
Cdd:PHA03095   110 VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
                          170       180
                   ....*....|....*....|..
gi 1622856719  271 PLHI---AIRGRSRKLAELLLR 289
Cdd:PHA03095   190 LLHHhlqSFKPRARIVRELIRA 211
PHA03095 PHA03095
ankyrin-like protein; Provisional
3-229 5.30e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 5.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTAL-MWACYKGRTDVVDLLLSHGANPSVTGLqYSVYPI-IWAAG-RGHADIVHLLLQNGAKVNCSDKYGTTPL-VWAA 78
Cdd:PHA03095    83 GFTPLhLYLYNATTLDVIKLLIKAGADVNAKDK-VGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLaVLLK 161
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   79 RKG-HLECVKHLLAMGADVDQEGANSMTAL---IVAVKgGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTE--IV 152
Cdd:PHA03095   162 SRNaNVELLRLLIDAGADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLV 240
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622856719  153 QDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTE 229
Cdd:PHA03095   241 LPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA02874 PHA02874
ankyrin repeat protein; Provisional
103-335 5.32e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.02  E-value: 5.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  103 SMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAG---TYVNIPDRSGDTVligavrg 179
Cdd:PHA02874    35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIPCIEKDMI------- 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  180 ghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGA 259
Cdd:PHA02874   108 ------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  260 KVSAVDKKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSILTQIFGARHLSPTETDG 335
Cdd:PHA02874   182 YANVKDNNGESPLHNAAEYGDYACIKLLIDH---GNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDIDG 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-293 1.05e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  206 LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAkvSAVDKKGDTPLHIAIRGRSRKLAE 285
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                   ....*...
gi 1622856719  286 LLLRNPKD 293
Cdd:pfam12796   79 LLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
50-275 1.25e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   50 ADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH---LECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEIL-KR 125
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  126 NPNVNLTDKDGNTALMI--ASKEGHTEIVQDLLDAGTYVNIPDRSGDT---VLIGAvRGGHVEIVRALLQKYADI---DI 197
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKS-RNANVELLRLLIDAGADVyavDD 185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  198 RGQdnkTALYWAVE--KGNATMVRDILQCNPDTEICTKDGETPLIKA---TKMRNIeVVELLLDKGAKVSAVDKKGDTPL 272
Cdd:PHA03095   186 RFR---SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRS-LVLPLLIAGISINARNRYGQTPL 261

                   ...
gi 1622856719  273 HIA 275
Cdd:PHA03095   262 HYA 264
PHA02875 PHA02875
ankyrin repeat protein; Provisional
3-197 1.54e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSVTglqysvYPIIW-----AAGRGHADIVHLLLQNGAKVN-CSDKYGTTPLVW 76
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK------YPDIEselhdAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHL 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   77 AARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 156
Cdd:PHA02875   109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1622856719  157 DAGTYVNIPDRSGD-TVLIGAVRGGHVEIVRALLQKYADIDI 197
Cdd:PHA02875   189 DSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
17-291 1.47e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   17 DVVDLLLSHGANPSVTG----------LQYSVYPIiwaagrghADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGH-LEC 85
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGeygktplhlyLHYSSEKV--------KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   86 VKHLLAMGADVDQEGANSMTALIVAVKGGYTQS--VKEILKRNPNVNLTDKDGNTAL--MIASKEGHTEIVQDLLDAGTY 161
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGAD 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  162 VNIPDRSGDTVLigavrggHV---------EIVRALLQKYADIDIRGQDNKTALYWAVEKGN--ATMVRDILQCNPDTEI 230
Cdd:PHA03095   180 VYAVDDRFRSLL-------HHhlqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINA 252
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622856719  231 CTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIR-GRSRKLAELLLRNP 291
Cdd:PHA03095   253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRnNNGRAVRAALAKNP 314
PHA02878 PHA02878
ankyrin repeat protein; Provisional
119-318 1.50e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 1.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  119 VKEILKRNPNVNLTDKDGNTAL--------MIASKEGHTEIVQDLLdAGTYVNIPDrsgdtvligAVRGGHVEIVRALLQ 190
Cdd:PHA02878    53 VKSLLTRGHNVNQPDHRDLTPLhiickepnKLGMKEMIRSINKCSV-FYTLVAIKD---------AFNNRNVEIFKIILT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  191 KYA----DIDIRGQDNKTAlywaVEKGNATMVRDILQCNPDTEICTKD-GETPLIKATKMRNIEVVELLLDKGAKVSAVD 265
Cdd:PHA02878   123 NRYkniqTIDLVYIDKKSK----DDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPD 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622856719  266 KKGDTPLHIAIRGRSRKLAELLLRNpkdGRLLYRPNKAGETPYNIDCSHQKSI 318
Cdd:PHA02878   199 KTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNTPLHISVGYCKDY 248
PHA02878 PHA02878
ankyrin repeat protein; Provisional
51-307 3.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 3.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   51 DIVHLLLQNGAKVNCSDKYGTTPLvwaarkgHLECvkhllamgADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 130
Cdd:PHA02878    51 DVVKSLLTRGHNVNQPDHRDLTPL-------HIIC--------KEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVE 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  131 -----LTDK-DGNTALMIA-----SKEG--HTEIVQDLLDAGTYVNIPDR-SGDTVLIGAVRGGHVEIVRALLQKYADID 196
Cdd:PHA02878   116 ifkiiLTNRyKNIQTIDLVyidkkSKDDiiEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  197 IRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPL-IKATKMRNIEVVELLLDKGAKVSAVDK-KGDTPLHI 274
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS 275
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1622856719  275 AIrgRSRKLAELLLRNPKDGRLLyrpNKAGETP 307
Cdd:PHA02878   276 SI--KSERKLKLLLEYGADINSL---NSYKLTP 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
15-266 3.78e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   15 RTDVVDLLLSHGANPSVTGLqYSVYPIiwaagrgH--------ADIVHLLLQNGAKVNCSDKYGTTPL-VWAARKG-HLE 84
Cdd:PHA03095    62 VKDIVRLLLEAGADVNAPER-CGFTPL-------HlylynattLDVIKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPK 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   85 CVKHLLAMGADVDQEGANSMTALIVAVK--GGYTQSVKEILKRNPNVNLTDKDGNTAL--MIASKEGHTEIVQDLLDAGT 160
Cdd:PHA03095   134 VIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGC 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  161 YVNIPDRSGDTVLIGAVRGGHVE--IVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETP 238
Cdd:PHA03095   214 DPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
                          250       260
                   ....*....|....*....|....*...
gi 1622856719  239 LIKATKMRNIEVVELLLDKGAKVSAVDK 266
Cdd:PHA03095   294 LSLMVRNNNGRAVRAALAKNPSAETVAA 321
COG4928 COG4928
Predicted P-loop ATPase, KAP-like [General function prediction only];
331-887 6.43e-13

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


Pssm-ID: 443956  Cd Length: 386  Bit Score: 71.87  E-value: 6.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  331 TETDGDMLGYDLYSSALADILSEPTMQPPICVGLYAQWGSGKSFLLKKLEDEMKTFAGqqieplfqfswlivfltlllcg 410
Cdd:COG4928      1 NETEEDLLGRKKYAESLANLIKSSDADEPLVIGLDGEWGSGKTSFLNLIEKELESNEK---------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  411 glgllfaftvhpnlgiavslsflallyifFIVIYFggrregeswnwawvlstrlarhigylelllklmfvNPpelpeqtt 490
Cdd:COG4928     59 -----------------------------VIVVYF-----------------------------------NA-------- 66
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  491 kalpvrFLFTDYNRLssvggetsLAEMIATLSDACEREfgflatrlfrvfKTEDTQGKKKWKKtcclpsfviflfiigcI 570
Cdd:COG4928     67 ------WLYDGEEDL--------LAALLSEIAAELEKK------------KKKDKKAAKKLKK----------------Y 104
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  571 ISGITLLAIfrvdpkhltvnavlisIASIVGLafvlncrtWWQVLDSLLNSQRKRLHNAASK-LHKLKSEgFMKVLKcev 649
Cdd:COG4928    105 AKRLSKLAL----------------KAGLLGG--------PAEAVAEALKALLKKEYKSKKKsIEAFREE-LEELLK--- 156
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  650 ELMARmaktidsftqnqtRLVVIIDGLDACEQDKVLQMLDTVRVLFSKGPFIAIFASDPHIIIKAINQNLNsvlrdSNIN 729
Cdd:COG4928    157 ELKGK-------------RLVVFIDDLDRCEPDEAIEVLELIKLFFDFPNVVFVLAFDREILEHALKERYG-----EDID 218
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  730 GHDYMRNIVHLPVFLNSRGLSNARKFLVTSATNGDVPcsdttGIQEDADRRVSQNSLGEMTKLGSKTALNRRDTYRRRQM 809
Cdd:COG4928    219 AREYLEKIIQVPFRLPPLSNELLILELDRLLELLLSA-----LLEALLALLLLRALAESISSLRAEFLLLLLLLKLELLL 293
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622856719  810 QRTITRQMSFDLTKLLVTEDW-FSDISPQTMRRLLNIVSVTGRLLRANQISFNWDRLASWINLTEQWPYRTSWLILYLE 887
Cdd:COG4928    294 ALLVLLLKLELLLENLLLAALlLLLDELELKKLLREDVASRASLYFINAELANLSLKLLKISSELLTLELKLEEERELS 372
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
51-219 8.83e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.98  E-value: 8.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   51 DIVHLLLQNGAKVNcsDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN 130
Cdd:PLN03192   508 NVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  131 LTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNiPDRSGDtVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAV 210
Cdd:PLN03192   586 IRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGD-LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663

                   ....*....
gi 1622856719  211 EKGNATMVR 219
Cdd:PLN03192   664 AEDHVDMVR 672
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-67 2.74e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.74e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHgANPSVTGLQYSvyPIIWAAGRGHADIVHLLLQNGAKVNCSD 67
Cdd:pfam12796   30 GRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT--ALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
17-257 9.39e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 69.09  E-value: 9.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   17 DVVDLLLShGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLV-----WAARKGHLECVKHLLA 91
Cdd:PHA02798    19 STVKLLIK-SCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   92 MGADVDQEGANSMTALIVAVKGGYTQSVKEIL---KRNPNVNLTDKDGNTALMIASKEGHT---EIVQDLLDAGTYVNIP 165
Cdd:PHA02798    98 NGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTH 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  166 -----------------DRSGDTVLIGAVRGGHV-------------EIVRALLQ--------------KYADIDIRGQD 201
Cdd:PHA02798   178 nnkekydtlhcyfkyniDRIDADILKLFVDNGFIinkenkshkkkfmEYLNSLLYdnkrfkknildfifSYIDINQVDEL 257
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  202 NKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDK 257
Cdd:PHA02798   258 GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK 313
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
103-310 1.25e-11

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: 68.89  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  103 SMTALIVAVKGGYTQSVKEILKrNPNVNLTDKD--GNTALMIASKEGHTEIVQDLLDAG-TYVNIPDRS----GDTVLIG 175
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLK-CPSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApELVNEPMTSdlyqGETALHI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  176 AVRGGHVEIVRALLQKYADID---------IRGQDNKtaLYWavekgnatmvrdilqcnpdteictkdGETPLIKATKMR 246
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVspratgtffRPGPKNL--IYY--------------------------GEHPLSFAACVG 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622856719  247 NIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLA----ELLLRNPKDGRL--LYR-PNKAGETPYNI 310
Cdd:cd22192    148 NEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpLDLvPNNQGLTPFKL 218
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
41-196 3.19e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 3.19e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   41 IIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYtQSVK 120
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH-HKIF 607
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  121 EILKR-----NPNVnltdkdGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADI 195
Cdd:PLN03192   608 RILYHfasisDPHA------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681

                   .
gi 1622856719  196 D 196
Cdd:PLN03192   682 D 682
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
107-265 5.64e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 5.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  107 LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVR 186
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  187 ALLQkYADIdirgQDNKTA---LYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSA 263
Cdd:PLN03192   609 ILYH-FASI----SDPHAAgdlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683

                   ..
gi 1622856719  264 VD 265
Cdd:PLN03192   684 AN 685
PHA02878 PHA02878
ankyrin repeat protein; Provisional
5-146 7.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 7.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    5 TALMWACYKGRTDVVDLLLSHGANPSVTGLQYSvYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWA-ARKGHL 83
Cdd:PHA02878   170 TALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDY 248
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622856719   84 ECVKHLLAMGADVD-QEGANSMTALIVAVKGgyTQSVKEILKRNPNVNLTDKDGNTALMIASKE 146
Cdd:PHA02878   249 DILKLLLEHGVDVNaKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-90 2.22e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 2.22e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622856719   40 PIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLL 90
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
14-162 1.31e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   14 GRTDVVDLLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMG 93
Cdd:PLN03192   536 GNAALLEELLKAKLDPDIGDSKGRT-PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFA 614
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622856719   94 ADVDQEGANSMtaLIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYV 162
Cdd:PLN03192   615 SISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA03100 PHA03100
ankyrin repeat protein; Provisional
16-163 1.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   16 TDVVDLLLSHGANPSVTglqysvypiiwaagrghaDIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGAD 95
Cdd:PHA03100   156 LKILKLLIDKGVDINAK------------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719   96 VDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVN--------LTDKDGNTALMIASKEgHTEIVQDLLDAGTYVN 163
Cdd:PHA03100   218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKtiietllyFKDKDLNTITKIKMLK-KSIMYMFLLDPGFYKN 292
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
3-156 2.85e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.18  E-value: 2.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGA---NPSVTG----------LQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY 69
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGAdvvSPRATGtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   70 GTTPLvwaarkghlecvkHLLAMGAdvDQEGANSMTALIVA-VKGGYTQSVKEIlkrnPNvnltdKDGNTALMIASKEGH 148
Cdd:cd22192    169 GNTVL-------------HILVLQP--NKTFACQMYDLILSyDKEDDLQPLDLV----PN-----NQGLTPFKLAAKEGN 224

                   ....*...
gi 1622856719  149 TEIVQDLL 156
Cdd:cd22192    225 IVMFQHLV 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
79-275 1.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   79 RKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDA 158
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  159 GTYVNIPDRSgdtvLIGAVRGGHVEIvrALLQKYADIDIRGQDN--KTALYWAVEKGN-ATMVRDILQCNPDTEICTKDG 235
Cdd:PHA02876   234 RSNINKNDLS----LLKAIRNEDLET--SLLLYDAGFSVNSIDDckNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKG 307
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1622856719  236 ETPL-IKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 275
Cdd:PHA02876   308 ETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
213-289 1.13e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.13e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622856719  213 GNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLR 289
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
151-307 1.65e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  151 IVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILqcnpDTEI 230
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRS 235
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622856719  231 CTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSrkLAELLLRNPKDGRLLYRPNKAGETP 307
Cdd:PHA02876   236 NINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPS--LSRLVPKLLERGADVNAKNIKGETP 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
182-290 2.23e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  182 VEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATmVRDILQC------NPDT-EICtkdGETPLIkaTKMRN---IEVV 251
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEK-VKDIVRLlleagaDVNApERC---GFTPLH--LYLYNattLDVI 100
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1622856719  252 ELLLDKGAKVSAVDKKGDTPLHIAIRGRS--RKLAELLLRN 290
Cdd:PHA03095   101 KLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRK 141
PHA02878 PHA02878
ankyrin repeat protein; Provisional
50-251 2.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 2.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   50 ADIVHLLLQNGAKVNCSDKY-GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPN 128
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  129 VNLTDKDGNTALMIASKE-GHTEIVQDLLDAGTYVNIPDR-SGDTVLIGAVRGGHVeiVRALLQKYADIDIRGQDNKTAL 206
Cdd:PHA02878   227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1622856719  207 YWAVEKGNATMVRDILQCNpdteICTKDGETPLIKATK--MRNIEVV 251
Cdd:PHA02878   305 SSAVKQYLCINIGRILISN----ICLLKRIKPDIKNSEgfIDNMDCI 347
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-189 4.17e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 4.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622856719  136 GNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGAVRGGHVEIVRALL 189
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
3-158 7.79e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 7.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSVTGLQYSVypIIW-AAGRGHADIVHLLLQNGAkvnCSDKY-GTTPLVWAARK 80
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT--ALWnAISAKHHKIFRILYHFAS---ISDPHaAGDLLCTAAKR 632
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   81 GHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNV---NLTDKDGNTAL--MIASKE-GHTEIVQD 154
Cdd:PLN03192   633 NDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTELreLLQKRElGHSITIVD 712

                   ....
gi 1622856719  155 LLDA 158
Cdd:PLN03192   713 SVPA 716
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-288 8.52e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 8.52e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622856719  237 TPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLL 288
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-156 1.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622856719  104 MTALIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLL 156
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
3-57 1.48e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSVTGLQySVYPIIWAAGRGHADIVHLLL 57
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
16-207 2.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   16 TDVVDLLLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGAD 95
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   96 VDQEGANSMTALIVAVkgGYTQS---VKEILKRNPNVNLTDK-DGNTALMIASKEghTEIVQDLLDAGTYVNIPDRSGDT 171
Cdd:PHA02878   227 TDARDKCGNTPLHISV--GYCKDydiLKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLT 302
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1622856719  172 VLIGAVRG------GHVEIVRALLQKYADIDIRG----QDNKTALY 207
Cdd:PHA02878   303 PLSSAVKQylciniGRILISNICLLKRIKPDIKNsegfIDNMDCIT 348
Ank_5 pfam13857
Ankyrin repeats (many copies);
56-110 3.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 3.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719   56 LLQNG-AKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVA 110
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
45-156 4.89e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 4.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   45 AGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADvdqegansmtalivavkggytqsvkeilk 124
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----------------------------- 140
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622856719  125 rnpnVNLTDKDGNTALMIASKEGHTEIVQDLL 156
Cdd:PTZ00322   141 ----PTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
70-120 4.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622856719   70 GTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVK 120
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
77-322 2.02e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.01  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   77 AARKGHLECVKHLLAMGADVDQEGANSM--TALIVAVKGGYTQSVKEILKRNPNVNLTdkdGNTALMIASKEGHtEIVQD 154
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKLNINCPDRLgrSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISLEYV-DAVEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  155 LL--------DAGTYVNIPDRSGD------TVLIGAVRGGHVEIVRALLQKYADIDIRGqdnktalywaveKGNATMVRD 220
Cdd:TIGR00870  100 ILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYEIVKLLLERGASVPARA------------CGDFFVKSQ 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  221 ILQcnpdteiCTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-----RGRSRKLA----ELLLR-- 289
Cdd:TIGR00870  168 GVD-------SFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefKAEYEELScqmyNFALSll 240
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622856719  290 -NPKDGRLLYR-PNKAGETPYNIDCSHQKSILTQI 322
Cdd:TIGR00870  241 dKLRDSKELEViLNHQGLTPLKLAAKEGRIVLFRL 275
Ank_5 pfam13857
Ankyrin repeats (many copies);
125-176 2.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622856719  125 RNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVLIGA 176
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
3-156 4.30e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 51.24  E-value: 4.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGAN-------------PSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY 69
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASvparacgdffvksQGVDSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   70 GTTplvwaarkghlecVKHLLAMGADVDQEG---ANSMTALIVAVKGG--YTQSVKEILKRnpnvnltdkDGNTALMIAS 144
Cdd:TIGR00870  208 GNT-------------LLHLLVMENEFKAEYeelSCQMYNFALSLLDKlrDSKELEVILNH---------QGLTPLKLAA 265
                          170
                   ....*....|..
gi 1622856719  145 KEGHTEIVQDLL 156
Cdd:TIGR00870  266 KEGRIVLFRLKL 277
PHA02946 PHA02946
ankyin-like protein; Provisional
110-310 9.20e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 9.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  110 AVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPDRSGDTVL--IGAVRGGHVEIVRA 187
Cdd:PHA02946    46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  188 LLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN--IEVVELLLDKGAKVSAVD 265
Cdd:PHA02946   126 LVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPD 205
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1622856719  266 KKGDTPLHIAIRGRSRKLAELLLRNPKDGrlLYRPNKAGETPYNI 310
Cdd:PHA02946   206 HDGNTPLHIVCSKTVKNVDIINLLLPSTD--VNKQNKFGDSPLTL 248
PHA02946 PHA02946
ankyin-like protein; Provisional
18-182 1.01e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   18 VVDLLLSHGANPSVTGlQYSVYPIIWAAGRGHADI--VHLLLQNGAKVNCS-DKYGTTPLVwAARKGHLECVKHLLAMGA 94
Cdd:PHA02946    87 IVAMLLTHGADPNACD-KQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSvDEEGCGPLL-ACTDPSERVFKKIMSIGF 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   95 D---VDQEGANSMTALIVAvKGGYTQSVKEILKRNPNVNLTDKDGNTAL-MIASKEGHTEIVQDLLDAGTYVNIPDRSGD 170
Cdd:PHA02946   165 EariVDKFGKNHIHRHLMS-DNPKASTISWMMKLGISPSKPDHDGNTPLhIVCSKTVKNVDIINLLLPSTDVNKQNKFGD 243
                          170
                   ....*....|....*
gi 1622856719  171 ---TVLIGAVRGGHV 182
Cdd:PHA02946   244 splTLLIKTLSPAHL 258
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
135-167 1.38e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622856719  135 DGNTALMIAS-KEGHTEIVQDLLDAGTYVNIPDR 167
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
3-32 1.58e-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: 1.58e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622856719    3 GWTALMWACYK-GRTDVVDLLLSHGANPSVT 32
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
3-31 1.61e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.61e-05
                            10        20
                    ....*....|....*....|....*....
gi 1622856719     3 GWTALMWACYKGRTDVVDLLLSHGANPSV 31
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
22-74 1.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622856719   22 LLSHGANPSVTGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPL 74
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02736 PHA02736
Viral ankyrin protein; Provisional
248-312 1.72e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 1.72e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  248 IEVVELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPKDGRLLYrpNKAGETPYNIDC 312
Cdd:PHA02736    71 QEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQPGVNMEIL--NYAFKTPYYVAC 134
PHA02884 PHA02884
ankyrin repeat protein; Provisional
16-108 2.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 48.06  E-value: 2.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   16 TDVVDLLLSHGANPSV---TGLQYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGT-TPLVWAARKGHLECVKHLLA 91
Cdd:PHA02884    46 TDIIDAILKLGADPEApfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLS 125
                           90
                   ....*....|....*..
gi 1622856719   92 MGADVDQEgANSMTALI 108
Cdd:PHA02884   126 YGADINIQ-TNDMVTPI 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
69-97 3.53e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.53e-05
                            10        20
                    ....*....|....*....|....*....
gi 1622856719    69 YGTTPLVWAARKGHLECVKHLLAMGADVD 97
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
69-98 7.04e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 7.04e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622856719   69 YGTTPLVWAA-RKGHLECVKHLLAMGADVDQ 98
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-255 7.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 7.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622856719  204 TALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVELLL 255
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
3-31 7.38e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 7.38e-05
                           10        20
                   ....*....|....*....|....*....
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSV 31
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
183-350 9.54e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  183 EIVRALLQ--------------KYADIDIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICTKD-------------- 234
Cdd:cd22194    111 EIVRILLAfaeengildrfinaEYTEEAYEGQ---TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  235 GETPLIKATKMRNIEVVELLLDKGAK-VSAVDKKGDTPLH----IAIRGRSR-----KLAELLLRNPKDGRLLYRPNKAG 304
Cdd:cd22194    188 GETPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHalvtVAEDSKTQndfvkRMYDMILLKSENKNLETIRNNEG 267
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622856719  305 ETPYNIDCSHQK-SILTQIFG-------ARHLSPTETDgdmLGYDLYSSALADI 350
Cdd:cd22194    268 LTPLQLAAKMGKaEILKYILSreikekpNRSLSRKFTD---WAYGPVSSSLYDL 318
PHA02875 PHA02875
ankyrin repeat protein; Provisional
202-336 9.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 9.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  202 NKTALYWAVEKGNATMVRDILQC--NPDTEIctKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAI-RG 278
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIgiNPNFEI--YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVeEG 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622856719  279 RSRKLAELLLRNPKDGRLLYrpnKAGETPYNIDCSHQKSILTQIFGARHLSPTETDGD 336
Cdd:PHA02875    80 DVKAVEELLDLGKFADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
51-156 1.01e-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: 46.68  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   51 DIVHLLLQNGAKVNCSDK--------------YGTTPLVWAARKGHLECVKHLLAMGADV----DQEGANSMTALIVAVK 112
Cdd:cd22194    155 DIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqDSRGNTVLHALVTVAE 234
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622856719  113 GGYTQ--SVKE----ILKRNPNVNL---TDKDGNTALMIASKEGHTEIVQDLL 156
Cdd:cd22194    235 DSKTQndFVKRmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02875 PHA02875
ankyrin repeat protein; Provisional
173-293 1.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  173 LIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRNIEVVE 252
Cdd:PHA02875     6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1622856719  253 LLLDKGAKVSAV-DKKGDTPLHIAIRGRSRKLAELLLRNPKD 293
Cdd:PHA02875    86 ELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
168-255 1.27e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  168 SGDTVliGAvrgghveivRALLQKYADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKATKMRN 247
Cdd:PTZ00322    92 SGDAV--GA---------RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160

                   ....*...
gi 1622856719  248 IEVVELLL 255
Cdd:PTZ00322   161 REVVQLLS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
3-156 1.31e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSV------------TGLQYSVYPIIWAAGRGHADIVHLLLQNGAK---VNCSD 67
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSAratgrffrkspgNLFYFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   68 KYGTTplvwaarkghlecVKHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALMI 142
Cdd:cd21882    153 SLGNT-------------VLHALVLQADNTPENSAFVCQmynllLSYGAHLDPTQQLEEI---------PNHQGLTPLKL 210
                          170
                   ....*....|....
gi 1622856719  143 ASKEGHTEIVQDLL 156
Cdd:cd21882    211 AAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
88-189 1.37e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   88 HLLAMGADVDQEGANSMTA-LIVAVKGGYTQSVKEILKRNPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTYVNIPD 166
Cdd:PTZ00322    66 HNLTTEEVIDPVVAHMLTVeLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
                           90       100
                   ....*....|....*....|...
gi 1622856719  167 RSGDTVLIGAVRGGHVEIVRALL 189
Cdd:PTZ00322   146 KDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-219 1.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622856719  169 GDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTALYWAVEKGNATMVR 219
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02878 PHA02878
ankyrin repeat protein; Provisional
238-323 2.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  238 PLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIAIRGRSRKLAELLLRNPKDGRLLYRPNKAGETPYNIDCSHQKS 317
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119

                   ....*.
gi 1622856719  318 ILTQIF 323
Cdd:PHA02878   120 ILTNRY 125
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
106-263 3.64e-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: 44.69  E-value: 3.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  106 ALIVAVKGGYTQSVKEILKRNP--NVNLTDKDGNTALMIASKEGHTEIVQDLLdagTYVNIPDRSGDTvLIGAVRGGHVE 183
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELL---LNLSCRGAVGDT-LLHAISLEYVD 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  184 IVRALLQKYADIDiRGQDNktaLYWAVEKGNATMVRDIlqcnpdteictkdgeTPLIKATKMRNIEVVELLLDKGAKVSA 263
Cdd:TIGR00870   96 AVEAILLHLLAAF-RKSGP---LELANDQYTSEFTPGI---------------TALHLAAHRQNYEIVKLLLERGASVPA 156
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
234-266 3.93e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.93e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622856719  234 DGETPLIKA-TKMRNIEVVELLLDKGAKVSAVDK 266
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-275 4.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622856719  221 ILQCNP-DTEICTKDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 275
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
40-68 5.49e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 5.49e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622856719   40 PIIWAAGR-GHADIVHLLLQNGAKVNCSDK 68
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
62-134 8.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.58  E-value: 8.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622856719   62 KVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQEGANSMTALIVAVKGGYTQSVKEILKRNPNVNLTDK 134
Cdd:PHA02989   248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKK 320
PHA02989 PHA02989
ankyrin repeat protein; Provisional
17-190 8.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.58  E-value: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   17 DVVDLLLSHGAN-PSVTGLQ-YSVYPIIWAAGRGHADIVHLLLQNGakVNCSDK---YGTTPLVWAARKG----HLECVK 87
Cdd:PHA02989   125 DMLRFLLSKGINvNDVKNSRgYNLLHMYLESFSVKKDVIKILLSFG--VNLFEKtslYGLTPMNIYLRNDidviSIKVIK 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   88 HLLAMGADVDQEGANSMTALIVAVKGGYTQSVKE------ILKRnPNVNLTDKDGNTALMIASKEGHTEIVQDLLDAGTY 161
Cdd:PHA02989   203 YLIKKGVNIETNNNGSESVLESFLDNNKILSKKEfkvlnfILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDD 281
                          170       180
                   ....*....|....*....|....*....
gi 1622856719  162 VNIPDRSGDTVLIGAVRGGHVEIVRALLQ 190
Cdd:PHA02989   282 IYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
3-156 1.33e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.87  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGA-------------NPSVTGLQYSVYPIIWAAGRGHADIVHLLLQN---GAKVNCS 66
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGAdvharasgeffkkKKGGPGFYFGELPLSLAACTNQLDIVKFLLENphsPADISAR 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   67 DKYGTTplvwaarkghlecVKHLLAMGADVDQEGANSMTALivavkggYTQSVKEILKRNPNVNL---TDKDGNTALMIA 143
Cdd:cd22196    174 DSMGNT-------------VLHALVEVADNTPENTKFVTKM-------YNEILILGAKIRPLLKLeeiTNKKGLTPLKLA 233
                          170
                   ....*....|...
gi 1622856719  144 SKEGHTEIVQDLL 156
Cdd:cd22196    234 AKTGKIGIFAYIL 246
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
72-97 1.64e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622856719   72 TPLVWAARKGHLECVKHLLAMGADVD 97
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
3-69 2.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 2.22e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSVTGLqYSVYPIIWAAGRGHADIVHLLLQNGAKVNCSDKY 69
Cdd:PHA03100   192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK-YGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
135-164 2.43e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.43e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622856719   135 DGNTALMIASKEGHTEIVQDLLDAGTYVNI 164
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
19-103 2.89e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   19 VDLLLSHGANPSVTGLQYSVyPIIWAAGRGHADIVHLLLQNGAKVNCSDKYGTTPLVWAARKGHLECVKHLLAMGADVDQ 98
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRT-PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176

                   ....*
gi 1622856719   99 EGANS 103
Cdd:PTZ00322   177 LGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
193-242 2.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.92e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622856719  193 ADIDIRGQDNKTALYWAVEKGNATMVRDILQCNPDTEICTKDGETPLIKA 242
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-206 3.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622856719  155 LLDAGTY-VNIPDRSGDTVLIGAVRGGHVEIVRALLQKYADIDIRGQDNKTAL 206
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
234-263 3.20e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.20e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622856719   234 DGETPLIKATKMRNIEVVELLLDKGAKVSA 263
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
251-310 3.75e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.41  E-value: 3.75e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622856719  251 VELLLDKGAKVSAVDKK-GDTPLHIAIRGRSRKLAELLLRNPkdGRLLYRPNKAGETPYNI 310
Cdd:PHA02743    76 IELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQL--GVNLGAINYQHETAYHI 134
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
169-197 4.14e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 4.14e-03
                            10        20
                    ....*....|....*....|....*....
gi 1622856719   169 GDTVLIGAVRGGHVEIVRALLQKYADIDI 197
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
3-156 5.30e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGANPSV------------TGLQYSVYPIIWAAGRGHADIVHLLLQNGAKvncsdkyg 70
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrffqkkqgTCFYFGELPLSLAACTKQWDVVNYLLENPHQ-------- 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   71 ttPLVWAARKGHLECVKHLLAMGADVDQEGansmTALIVAVkggYTQSVKEILKRNPNVNL---TDKDGNTALMIASKEG 147
Cdd:cd22197    166 --PASLQAQDSLGNTVLHALVMIADNSPEN----SALVIKM---YDGLLQAGARLCPTVQLeeiSNHEGLTPLKLAAKEG 236

                   ....*....
gi 1622856719  148 HTEIVQDLL 156
Cdd:cd22197    237 KIEIFRHIL 245
PHA02791 PHA02791
ankyrin-like protein; Provisional
196-308 5.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719  196 DIRGQdnkTALYWAVEKGNATMVRDILQCNPDTEICtkDGETPLIKATKMRNIEVVELLLDKGAKVSAVDKKGDTPLHIA 275
Cdd:PHA02791    27 DVHGH---SALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYA 101
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1622856719  276 IRGRSRKLAELLLRnpKDGRLLYRPNKAGETPY 308
Cdd:PHA02791   102 VDSGNMQTVKLFVK--KNWRLMFYGKTGWKTSF 132
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
3-156 5.39e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 5.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719    3 GWTALMWACYKGRTDVVDLLLSHGA-----------NPSV--TGLQYSVYPIIWAAGRGHADIVHLLLQNG---AKVNCS 66
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGAdvhahakgrffQPKYqgEGFYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622856719   67 DKYGTTPLvwaarkghlecvkHLLAMGADVDQEGANSMTA-----LIVAVKGGYTQSVKEIlkrnpnvnlTDKDGNTALM 141
Cdd:cd22193    156 DSRGNTVL-------------HALVTVADNTKENTKFVTRmydmiLIRGAKLCPTVELEEI---------RNNDGLTPLQ 213
                          170
                   ....*....|....*
gi 1622856719  142 IASKEGHTEIVQDLL 156
Cdd:cd22193    214 LAAKMGKIEILKYIL 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
169-198 5.43e-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. 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: 5.43e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1622856719  169 GDTVL-IGAVRGGHVEIVRALLQKYADIDIR 198
Cdd:pfam00023    2 GNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
40-65 7.25e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 7.25e-03
                            10        20
                    ....*....|....*....|....*.
gi 1622856719    40 PIIWAAGRGHADIVHLLLQNGAKVNC 65
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
 
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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