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Conserved domains on  [gi|116063534|ref|NP_115515|]
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ankyrin repeat domain-containing protein 27 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-932 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  673 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 752
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  753 LHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQH 832
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  833 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQ--NSKIMELLQVVPSCVASLDDVAETD 910
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                         250       260
                  ....*....|....*....|..
gi 116063534  911 RKEYVTVKIRKKWNSKLYDLPD 932
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.46e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063534  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 6.60e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


:

Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 83.46  E-value: 6.60e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 116063534  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 2.99e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


:

Pssm-ID: 460489  Cd Length: 104  Bit Score: 78.02  E-value: 2.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSL 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 116063534   344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-932 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  673 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 752
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  753 LHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQH 832
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  833 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQ--NSKIMELLQVVPSCVASLDDVAETD 910
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                         250       260
                  ....*....|....*....|..
gi 116063534  911 RKEYVTVKIRKKWNSKLYDLPD 932
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.46e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063534  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-873 2.32e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.18  E-value: 2.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   781 LHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHgASINASNNkGNTALHEAVIEKHVFVVE 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 116063534   861 LLLLHGASVQVLN 873
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 4.73e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 4.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   500 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 116063534   580 VIETLLQNGASTEIQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 734-874 1.12e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVAALH--GRADLIPLLLKHGANAGARNADQAVPLHLACQQGH--FQVVKCLLDSNAKPNKK--- 806
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrv 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  807 -------------DLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLN 873
Cdd:PHA03100  176 nyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                  .
gi 116063534  874 K 874
Cdd:PHA03100  256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 6.60e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 83.46  E-value: 6.60e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 116063534  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 5.98e-18

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 78.14  E-value: 5.98e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116063534  706 ADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 747
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 2.99e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 78.02  E-value: 2.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSL 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 116063534   344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-626 5.21e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  460 DDRGHTPLHVAAVC--GQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 519
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  520 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 596
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 116063534  597 -LKETPLKCALNSKIL--SVMEAYHL--SFERRQK 626
Cdd:PHA03100  260 yFKDKDLNTITKIKMLkkSIMYMFLLdpGFYKNRK 294
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 371-586 1.31e-09

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: 62.12  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  371 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDTVqkmchplcfcddceklvsg 446
Cdd:cd22193     1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  447 rlnDPSVVTPFsRDD--RGHTPLHVAAVCGQASLIDLLVSKGAMVNATD--------------YHGATPLHL-ACQKGYQ 509
Cdd:cd22193    62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  510 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 572
Cdd:cd22193   138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                         250
                  ....*....|....
gi 116063534  573 ARWGYQGVIETLLQ 586
Cdd:cd22193   216 AKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 2.49e-08

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: 58.17  E-value: 2.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   449 NDPSvvtpFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNA------------TD--YHGATPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   515 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 116063534   581 IETLLQ 586
Cdd:TIGR00870  273 FRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 2.28e-07

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 50.53  E-value: 2.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534    264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSL 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 116063534    344 AKDELGYCLTSFEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-838 2.33e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.33e-06
                            10        20
                    ....*....|....*....|....*....
gi 116063534    810 GNTPLIYACSGGHHELVALLLQHGASINA 838
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 744-889 1.15e-05

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: 49.31  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   744 GSSPLHVAALHGRADLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKCLLDSnakpnkkdLS-GNTPL-IYACSGg 821
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   822 HHELVALLLQHGASINASNNKGNTALHEAVIEKHV-------------FVVELLLLHGASVQ---VLNKRQRTAVDCAEQ 885
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmynFALSLLDKLRDSKElevILNHQGLTPLKLAAK 266


                   ....
gi 116063534   886 NSKI 889
Cdd:TIGR00870  267 EGRI 270
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-554 3.45e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.45e-05
                            10        20
                    ....*....|....*....|....*..
gi 116063534    528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-932 1.03e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.28  E-value: 1.03e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  673 LLRAVADGDLEMVRYLLEWTEEDLEDAEDTVSAADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 752
Cdd:COG0666    16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  753 LHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQH 832
Cdd:COG0666    96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  833 GASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQ--NSKIMELLQVVPSCVASLDDVAETD 910
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                         250       260
                  ....*....|....*....|..
gi 116063534  911 RKEYVTVKIRKKWNSKLYDLPD 932
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-879 5.50e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 5.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  476 ASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVEs 555
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  556 crLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLkcalnskilsvmeayhlsferrqksseapvqsp 635
Cdd:COG0666    80 --INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  636 qrsvdsisqesstssfssmsassrqeetkkdyreveklLRAVADGDLEMVRYLLEwteedledaedtvSAADpefchplc 715
Cdd:COG0666   125 --------------------------------------HLAAYNGNLEIVKLLLE-------------AGAD-------- 145

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  716 qcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKC 795
Cdd:COG0666   146 ---------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  796 LLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKR 875
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                  ....
gi 116063534  876 QRTA 879
Cdd:COG0666   285 LLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.46e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.46e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063534  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEA 616
Cdd:COG0666   163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
460-847 1.26e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 1.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  460 DDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTY 539
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  540 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLkcalnskilsvmeayhl 619
Cdd:COG0666    98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL----------------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  620 sferrqksseapvqspqrsvdsisqesstssfssmsassrqeetkkdyreveklLRAVADGDLEMVRYLLEwteedleda 699
Cdd:COG0666   158 ------------------------------------------------------HLAAANGNLEIVKLLLE--------- 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  700 edtvSAADpefchplcqcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAV 779
Cdd:COG0666   175 ----AGAD-----------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063534  780 PLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTAL 847
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-611 8.60e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 8.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKIL 611
Cdd:COG0666   196 NGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-893 1.89e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  725 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPN 804
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  805 KKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA- 883
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161

                         170
                  ....*....|.
gi 116063534  884 -EQNSKIMELL 893
Cdd:COG0666   162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-873 2.32e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.18  E-value: 2.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   781 LHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHgASINASNNkGNTALHEAVIEKHVFVVE 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 116063534   861 LLLLHGASVQVLN 873
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-840 1.31e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.31e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   748 LHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDsNAKPNKKDlSGNTPLIYACSGGHHELVA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 116063534   828 LLLQHGASINASN 840
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 4.73e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 4.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   500 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 116063534   580 VIETLLQNGASTEIQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 734-874 1.12e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.89  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVAALH--GRADLIPLLLKHGANAGARNADQAVPLHLACQQGH--FQVVKCLLDSNAKPNKK--- 806
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrv 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  807 -------------DLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLN 873
Cdd:PHA03100  176 nyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                  .
gi 116063534  874 K 874
Cdd:PHA03100  256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 6.60e-20

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 83.46  E-value: 6.60e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 116063534  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 5.98e-18

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 78.14  E-value: 5.98e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 116063534  706 ADPEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 747
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 2.99e-17

Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). It activates Rab GTPases by stimulating the release of GDP and allowing GTP to bind.


Pssm-ID: 460489  Cd Length: 104  Bit Score: 78.02  E-value: 2.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSL 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 116063534   344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-554 3.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   467 LHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEvqDNNGNTPLHLACTYGHEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 116063534   547 ALVYYDVE 554
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 738-872 5.40e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 5.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  738 NVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYA 817
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534  818 CSGGHHELVALLLQHGASINASNNKGN-TALHEAVIEKHVFVVELLLLHGASVQVL 872
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-626 5.21e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  460 DDRGHTPLHVAAVC--GQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 519
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  520 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 596
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 116063534  597 -LKETPLKCALNSKIL--SVMEAYHL--SFERRQK 626
Cdd:PHA03100  260 yFKDKDLNTITKIKMLkkSIMYMFLLdpGFYKNRK 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 480-874 6.90e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.42  E-value: 6.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  480 DLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVyydveSCRLD 559
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  560 IgnEKGDTPLHIAARwgyQGVIET---LLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLsferrqksseapvqspQ 636
Cdd:PHA02876  237 I--NKNDLSLLKAIR---NEDLETsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLL----------------E 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  637 RSVDSisqesstssfssmsassrqeETKKDYREVEKLLRAVADGDLEMVRYLLEWTEEdledaedtVSAADPEFCHPLCQ 716
Cdd:PHA02876  296 RGADV--------------------NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQ 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  717 CPKCAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLA-CQQGHFQVVKC 795
Cdd:PHA02876  348 ASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKT 427

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  796 LLDSNAKPNKKDLSGNTPLIYACSGG-HHELVALLLQHGASINASNNKGNTALHEAvIEKHVfVVELLLLHGASV---QV 871
Cdd:PHA02876  428 LIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAELrdsRV 505


                  ...
gi 116063534  872 LNK 874
Cdd:PHA02876  506 LHK 508
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 733-863 1.03e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  733 SGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNT 812
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 116063534  813 PLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVfVVELLL 863
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-548 1.08e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                          90
                  ....*....|
gi 116063534  539 YGHEDCVKAL 548
Cdd:COG0666   262 AGAALIVKLL 271
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 732-883 2.76e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  732 ASGLGVNVTSQD-GSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSG 810
Cdd:PHA02878  155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063534  811 NTPLIYACSG-GHHELVALLLQHGASINA-SNNKGNTALHEAVIEKHvfVVELLLLHGASVQVLNKRQRTAVDCA 883
Cdd:PHA02878  235 NTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 4.23e-15

Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails.


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 69.98  E-value: 4.23e-15
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 116063534  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 725-874 5.40e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  725 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-----VVKCLLDS 799
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  800 NAKPNKKDLSGNTPLIYACSG--GHHELVALLLQHGASINASNNKGNTALHEAVIEKHV--FVVELLLLHGASVQVLNK 874
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 459-607 9.97e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 9.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:PHA02874  120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  539 YGHEDCVKALVyydVESCRLDIGNEKGDTPLHIAARWGyQGVIEtLLQNGASTEIQNRLKETPLKCALN 607
Cdd:PHA02874  200 YGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHN-RSAIE-LLINNASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 459-606 1.65e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKG-YQSVTLLLLHyKASAEVQDNNGNTPLHLAC 537
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  538 TYGhedcvKALVYYDVESCRLDIGNEKGDTPLHIAARWG-YQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02874  232 IHN-----RSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAF 296
PHA03095 PHA03095
ankyrin-like protein; Provisional
 756-882 6.64e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 6.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  756 RADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ---VVKCLLDSNAKPNKKDLSGNTPLI-YACSGGHHELVALLLQ 831
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 116063534  832 HGASINASNNKGNTALHE--AVIEKHVFVVELLLLHGASVQVLNKRQRTAVDC 882
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 734-933 8.21e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 8.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTP 813
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  814 LIYACSggHHELVALLLQHGASINASNNKGNTALHEAVIEK-HVFVVELLLLHGASVQVLNKRQRTAVDCAEQNSKIMEL 892
Cdd:PHA02874  227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV 304

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 116063534  893 LQ-VVPSCV--ASLDDVAETDRKEYVTVKIRKKWNSKLYDLPDE 933
Cdd:PHA02874  305 IKdIIANAVliKEADKLKDSDFLEHIEIKDNKEFSDFIKECNEE 348
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 733-871 9.60e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.64  E-value: 9.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  733 SGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNK---KDls 809
Cdd:PHA02875   24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD-- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116063534  810 GNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQV 871
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-896 1.64e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  567 TPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYhlsferrqksseapvqspqrsVDSisqes 646
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI---------------------IDN----- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  647 stssfssmsassRQEETKKDYreveKLLRAVADGDLEmvryllewTEEDLEDAEDTVSAADPEFCHPLCQCPKcAPAQKR 726
Cdd:PHA02876  234 ------------RSNINKNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQ-APSLSR 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  727 LA-KVPASGLGVNVTSQDGSSPLHVAALHG-RADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-VVKCLLDSNAKP 803
Cdd:PHA02876  289 LVpKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANV 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  804 NKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFV-VELLLLHGASVQVLNKRQRTAVDC 882
Cdd:PHA02876  369 NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHY 448

                         330
                  ....*....|....
gi 116063534  883 AEQNSKIMELLQVV 896
Cdd:PHA02876  449 ACKKNCKLDVIEML 462
PHA03095 PHA03095
ankyrin-like protein; Provisional
 681-848 2.19e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  681 DLEMVRYLLEwteedlEDAedTVSAADPEFCHPLCQCPKCApAQKRLAKVPA---SGLGVNVTSQDGSSPLHVAALHG-R 756
Cdd:PHA03095   26 TVEEVRRLLA------AGA--DVNFRGEYGKTPLHLYLHYS-SEKVKDIVRLlleAGADVNAPERCGFTPLHLYLYNAtT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  757 ADLIPLLLKHGANAGARNADQAVPLH--LACQQGHFQVVKCLLDSNAKPNKKDLSGNTPL-IYACSGGHH-ELVALLLQH 832
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvELLRLLIDA 176

                         170
                  ....*....|....*.
gi 116063534  833 GASINASNNKGNTALH 848
Cdd:PHA03095  177 GADVYAVDDRFRSLLH 192
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 478-613 2.38e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  478 LIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTL--LLLHYKASAEVQDNNGNTPLHLACTYGHED--CVKALVYYDV 553
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGV 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  554 E-------------SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSV 613
Cdd:PHA03100  168 DinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 481-863 3.03e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  481 LLVSKGAMVNATDYHGATPLHLACQKGYQSVT---LLLLHYKASAEVQDNNGNTPLHLACTYGH-EDCVKALVYY--DVE 554
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  555 SCrldigNEKGDTPLHIAAR--WGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKilsvmeayhlsferrqksseapv 632
Cdd:PHA03095  112 AK-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR----------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  633 qspqrsvdsisqesstssfssmsassrqeetkkdyrevekllravaDGDLEMVRYLLEwteedledaedtvsaadpefch 712
Cdd:PHA03095  164 ----------------------------------------------NANVELLRLLID---------------------- 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  713 plcqcpkcapaqkrlakvpasgLGVNVTSQD--GSSPLHVAA--LHGRADLIPLLLKHGANAGARNADQAVPLHLACQQG 788
Cdd:PHA03095  176 ----------------------AGADVYAVDdrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS 233

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116063534  789 HFQ--VVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 863
Cdd:PHA03095  234 SCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 3.20e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.38  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  461 DRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYg 540
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  541 hedcvkaLVYYDVESCRLDIG---NEK----GDTPLHIAARwgYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02878  245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 758-893 5.58e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  758 DLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASIN 837
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116063534  838 ASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA-EQNSKIMELL 893
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELL 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
673-807 6.86e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 6.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   673 LLRAVADGDLEMVRYLLEwteedledaedtvsaadpefchplcqcpkcapaqkrlakvpaSGLGVNVTSQDGSSPLHVAA 752
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE------------------------------------------NGADANLQDKNGRTALHLAA 38

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 116063534   753 LHGRADLIPLLLKHgANAGARNADQAvPLHLACQQGHFQVVKCLLDSNAKPNKKD 807
Cdd:pfam12796   39 KNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 776-893 1.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  776 DQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHH-----ELVALLLQHGASINASNNKGNTALHEA 850
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 116063534  851 VIEK--HVFVVELLLLHGASVQVLNKRQRT----AVDCAEQNSKIMELL 893
Cdd:PHA03100  114 ISKKsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PHA03095 PHA03095
ankyrin-like protein; Provisional
 459-602 2.13e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHV--AAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEV--QDNNGNTPLH 534
Cdd:PHA03095  113 KDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyaVDDRFRSLLH 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116063534  535 LACTYGH--EDCVKALVyydVESCRLDIGNEKGDTPLHIAARWGY--QGVIETLLQNGASTEIQNRLKETPL 602
Cdd:PHA03095  193 HHLQSFKprARIVRELI---RAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPL 261
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 709-747 3.08e-12

Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails.


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 61.89  E-value: 3.08e-12
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 116063534  709 EFCHPLCQCPKCAPAQKRLAKVPaSGLGVNVTSQDGSSP 747
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDP-SGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-608 4.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.52  E-value: 4.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  475 QASLIDLLVSKGAMVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdv 553
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  554 eSCRLDIGNEKGDTPLHIAArwGY---QGVIETLLQNGASTEIQNRLKE-TPLKCALNS 608
Cdd:PHA02878  224 -GASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 471-559 5.15e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.93  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  471 AVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVY 550
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                  ....*....
gi 116063534  551 YDVESCRLD 559
Cdd:PTZ00322  170 HSQCHFELG 178
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 473-606 8.03e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 8.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  473 CGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYyd 552
Cdd:PHA02874  101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-- 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 116063534  553 vESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02874  179 -KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
757-893 8.90e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  757 ADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASI 836
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  837 NASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA--EQNSKIMELL 893
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayNGNLEIVKLL 139
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 724-873 2.34e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  724 QKRLAKVPASGLGVNVTSQDG----SSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDS 799
Cdd:PLN03192  501 HKELHDLNVGDLLGDNGGEHDdpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  800 NAKPNKKDLSGNTPLIYACSGGHHELVAL-------------------------------LLQHGASINASNNKGNTALH 848
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHHKIFRIlyhfasisdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQ 660

                         170       180
                  ....*....|....*....|....*
gi 116063534  849 EAVIEKHVFVVELLLLHGASVQVLN 873
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 2.95e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.95e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116063534   456 PFSRDDRGHTPLHVAAVCGQASLIDLLVSKgAMVNATDYhGATPLHLACQKGYQSVTLLLLHYKASAEVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
810-863 4.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 116063534   810 GNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 863
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 673-850 5.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  673 LLRAVADGDLEMVRYLLEWTEEdledaedtVSAADPEFCHPLCQCPKcAPAQKRLAKVPASGLGVNVTSQDGSSPLHVAA 752
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIK-HNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  753 LHGRADLIPLLLKHGANAGARNADQAVPLHLACQqgHFQVVKCLLDSNAKPNKKDLSGNTPLIYA----CSgghHELVAL 828
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDI 273

                         170       180
                  ....*....|....*....|..
gi 116063534  829 LLQHGASINASNNKGNTALHEA 850
Cdd:PHA02874  274 LLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 463-613 2.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  463 GHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKG-YQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 541
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116063534  542 EDCVKALVYYDVEScrlDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSV 613
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 749-832 3.67e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  749 HVAAlHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVAL 828
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....
gi 116063534  829 LLQH 832
Cdd:PTZ00322  167 LSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 734-869 3.90e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVAALHGRAD--LIPLLLKHGANAGARNADQAVPLHLACQQGH--FQVVKCLLDSNAKPNKKDLS 809
Cdd:PHA03095  142 GADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDML 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  810 GNTPLIYACSGG--HHELVALLLQHGASINASNNKGNTALHEAVI-EKHVFVVELLLLhGASV 869
Cdd:PHA03095  222 GNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVfNNPRACRRLIAL-GADI 283
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 465-604 4.53e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 4.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  465 TPLHVAAVCGQASLIDLLVSKGAMVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHED 543
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116063534  544 CVKALVyyDVESCrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKC 604
Cdd:PHA02875  150 GIELLI--DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
PHA02798 PHA02798
ankyrin-like protein; Provisional
 758-882 1.16e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.16  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  758 DLIPLLLKHGANAGARNADQAVPL-----HLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGH---HELVALL 829
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFM 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116063534  830 LQHGASINASNNKGNTALHEAVIEKH---VFVVELLLLHGASV-QVLNKRQRTAVDC 882
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDInTHNNKEKYDTLHC 188
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 371-586 1.31e-09

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: 62.12  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  371 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDTVqkmchplcfcddceklvsg 446
Cdd:cd22193     1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  447 rlnDPSVVTPFsRDD--RGHTPLHVAAVCGQASLIDLLVSKGAMVNATD--------------YHGATPLHL-ACQKGYQ 509
Cdd:cd22193    62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  510 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 572
Cdd:cd22193   138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                         250
                  ....*....|....
gi 116063534  573 ARWGYQGVIETLLQ 586
Cdd:cd22193   216 AKMGKIEILKYILQ 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 466-608 1.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  466 PLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQ---------------------------------------- 505
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  506 ------KGYQS------------------VTLLLLHYKASAEVQD-NNGNTPLHLACTYGHEDCVKALVYYDVESCRLDI 560
Cdd:PHA02878  120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 116063534  561 GNekgDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNS 608
Cdd:PHA02878  200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
Ank_4 pfam13637
Ankyrin repeats (many copies);
780-830 1.70e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.70e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 116063534   780 PLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLL 830
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 736-911 2.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  736 GVNVTSQD--GSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSgntp 813
Cdd:PHA02876  168 GADVNAKDiyCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  814 LIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVF-VVELLLLHGASVQVLNKRQRTAVDCAEQNSKIMEL 892
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEN 323

                         170
                  ....*....|....*....
gi 116063534  893 LQVVPSCVAsldDVAETDR 911
Cdd:PHA02876  324 IRTLIMLGA---DVNAADR 339
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-606 2.84e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  470 AAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 549
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116063534  550 YYdvesCRLDIGNEKGDTpLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PLN03192  612 HF----ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
Ank_4 pfam13637
Ankyrin repeats (many copies);
744-797 3.15e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 116063534   744 GSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLL 797
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 734-909 5.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVA------------------------------ALHGR--------------------------- 756
Cdd:PHA02878   60 GHNVNQPDHRDLTPLHIIckepnklgmkemirsinkcsvfytlvaikdAFNNRnveifkiiltnrykniqtidlvyidkk 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  757 -------ADLIPLLLKHGA--NAGARNADQAvPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVA 827
Cdd:PHA02878  140 skddiieAEITKLLLSYGAdiNMKDRHKGNT-ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  828 LLLQHGASINASNNKGNTALHEAVIE-KHVFVVELLLLHGASVQVLNK-RQRTAVDCAEQNSKIMELLQVVPSCVASLDD 905
Cdd:PHA02878  219 ILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNS 298


                  ....
gi 116063534  906 VAET 909
Cdd:PHA02878  299 YKLT 302
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 744-848 6.77e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 6.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  744 GSSPLHVAALHGRADLIPLLLkhgaNAGARNADQAV---------PLHLACQQGHFQVVKCLLDSNA------------K 802
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLM----EAAPELVNEPMtsdlyqgetALHIAVVNQNLNLVRELIARGAdvvspratgtffR 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 116063534  803 PNKKDLS--GNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALH 848
Cdd:cd22192   127 PGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-606 8.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 8.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  458 SRDDRGHTPLHVAAVCGQAS-LIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTL-LLLHYKASAEVQDNNGNTPLHL 535
Cdd:PHA02876  268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116063534  536 ACTYG-HEDCVKALVYYDVESCRLDIGNEkgdTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02876  348 ASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PHA03095 PHA03095
ankyrin-like protein; Provisional
 459-602 9.10e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 9.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVAAVCGQAS--LIDLLVSKGAMVNATDYHGATPLHLACQ--KGYQSVTLLLLHYKASAEVQDNNGNTPLH 534
Cdd:PHA03095  148 LDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLH 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  535 LACTYGheDCVKALVYYDVES-CRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 602
Cdd:PHA03095  228 SMATGS--SCKRSLVLPLLIAgISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 383-594 1.00e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.12  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  383 LKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDTVQKMCHPLCFCDDCEKLVsgrlNDPSVVTPFsrddR 462
Cdd:cd21882     1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELV----NAPCTDEFY----Q 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  463 GHTPLHVAAVCGQASLIDLLVSKGAMVNATD-------------YHGATPLHL-ACQKGYQSVTLLLLH--YKASAEVQD 526
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  527 NNGNTPLH--------------LACTYGHEdcvkaLVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGVIETLLQNG 588
Cdd:cd21882   153 SLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227


                  ....*.
gi 116063534  589 ASTEIQ 594
Cdd:cd21882   228 FSGPYQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
498-549 1.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.59e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 116063534   498 TPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 549
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 732-837 1.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  732 ASGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGN 811
Cdd:PHA02875  123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                          90       100
                  ....*....|....*....|....*..
gi 116063534  812 -TPLIYACSGGHHELVALLLQHGASIN 837
Cdd:PHA02875  203 vAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 2.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 2.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534   482 LVSKGAM-VNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 2.49e-08

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: 58.17  E-value: 2.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   449 NDPSvvtpFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNA------------TD--YHGATPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   515 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 116063534   581 IETLLQ 586
Cdd:TIGR00870  273 FRLKLA 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 456-547 4.80e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 4.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  456 PFSRDDRGHTPLHVAAVCG--QASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPL 533
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                          90
                  ....*....|....
gi 116063534  534 HLACTYGHEDCVKA 547
Cdd:PHA03095  295 SLMVRNNNGRAVRA 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 465-606 4.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 4.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  465 TPLHVAAVCGQ-ASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA-CTYGHE 542
Cdd:PHA02876  343 TPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063534  543 DCVKALVYydvESCRLDIGNEKGDTPLHIAARWGYQ-GVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02876  423 MSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 7.57e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 7.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  461 DRGHTPLHVAAVCGQaSLIDLLVSKgAMVNATDYHGATPLHLA----CQKgyqSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:PHA02874  221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                  ....*....
gi 116063534  537 CTYGHEDCV 545
Cdd:PHA02874  296 FKYINKDPV 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-549 8.08e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  462 RGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 541
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  ....*...
gi 116063534  542 EDCVKALV 549
Cdd:PHA02875  181 IAICKMLL 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 734-851 9.92e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 9.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  734 GLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQ-GHFQVVKCLLDSNAKPNKKD-LSGN 811
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGL 270

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 116063534  812 TPLIYACSGghHELVALLLQHGASINASNNKGNTALHEAV 851
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-850 1.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 116063534   803 PNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEA 850
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 2.28e-07

Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.


Pssm-ID: 128469  Cd Length: 117  Bit Score: 50.53  E-value: 2.28e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534    264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSL 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 116063534    344 AKDELGYCLTSFEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 793-865 3.55e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  793 VKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLH 865
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 3.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 116063534   529 GNTPLHLACTYGHEDCVKALVYYDVESCRLDIGnekGDTPLHIAARWGYQGVIETLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 3.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 3.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  459 RDDRGHTPLHVA-AVCGQASLIDLLVSKGAMVNATDY-HGATPLHLACQKgyQSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90       100
                  ....*....|....*....|....*.
gi 116063534  537 ctyghedcvkALVYYDVESCRLDIGN 562
Cdd:PHA02878  308 ----------VKQYLCINIGRILISN 323
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 3.95e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.95e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534   514 LLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
463-516 1.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.03e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 116063534   463 GHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLL 516
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-841 1.03e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 116063534   810 GNTPLIYAC-SGGHHELVALLLQHGASINASNN 841
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 1.05e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  463 GHTPLHVAAVCGQASLIDLLVSKGAMVN---ATD-----------YHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 528
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116063534  529 GNTPLH---------LAC-TYgheDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQN 587
Cdd:cd22192   169 GNTVLHilvlqpnktFACqMY---DLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 470-615 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  470 AAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGheDCVKALV 549
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG--DVKAVEE 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534  550 YYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVME 615
Cdd:PHA02875   87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
Ank_5 pfam13857
Ankyrin repeats (many copies);
737-784 1.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.90e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 116063534   737 VNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLA 784
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-838 2.33e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 2.33e-06
                            10        20
                    ....*....|....*....|....*....
gi 116063534    810 GNTPLIYACSGGHHELVALLLQHGASINA 838
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 2.57e-06

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: 51.39  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  462 RGHTPLHVAAVCGQASLIDLLVSKGAMVNATD-------------YHGATPLHL-ACQKGYQSVTLLL--LHYKASAEVQ 525
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063534  526 DNNGNTPLHlACTYGHEDCVK--ALV--YYD---VESCRLD-------IGNEKGDTPLHIAARWGYQGVIETLLQ 586
Cdd:cd22197   173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDgllQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 462-576 3.10e-06

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: 51.30  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  462 RGHTPLHVAAVCGQASLIDLLVSKGAMVNATD--------------YHGATPLHL-ACQKGYQSVTLLLLHYKASAEVQD 526
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116063534  527 NNGNTPLHLACTYG-----HEDCVKALvyYDV-----ESCRLD-IGNEKGDTPLHIAARWG 576
Cdd:cd22194   220 SRGNTVLHALVTVAedsktQNDFVKRM--YDMillksENKNLEtIRNNEGLTPLQLAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 456-518 3.75e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  456 PFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHY 518
Cdd:PTZ00322  108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 460-595 6.74e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  460 DDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQdnNGNTPLHLACTY 539
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKR 632

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534  540 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQN 595
Cdd:PLN03192  633 NDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 458-528 8.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 8.40e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116063534  458 SRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 528
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 398-595 1.13e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.42  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  398 TDCLFKHIASGNQKEVERLLSQEDHDKDTVqkmchpLCFCDDCEKlvSGRLNDpsVVTPFSRDD--RGHTPLHVAAVCGQ 475
Cdd:cd22196    37 TDSEFKDPETGKTCLLKAMLNLHNGQNDTI------SLLLDIAEK--TGNLKE--FVNAAYTDSyyKGQTALHIAIERRN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  476 ASLIDLLVSKGAMVNATD--------------YHGATPLHL-ACQKGYQSVTLLLL--HYKASAEVQDNNGNTPLHLACT 538
Cdd:cd22196   107 MHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISARDSMGNTVLHALVE 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116063534  539 YG--------------HEDCVKALVYYDVESCRlDIGNEKGDTPLHIAARWGYQGVIETLLQNgastEIQN 595
Cdd:cd22196   187 VAdntpentkfvtkmyNEILILGAKIRPLLKLE-EITNKKGLTPLKLAAKTGKIGIFAYILGR----EIKE 252
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 744-889 1.15e-05

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: 49.31  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   744 GSSPLHVAALHGRADLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKCLLDSnakpnkkdLS-GNTPL-IYACSGg 821
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534   822 HHELVALLLQHGASINASNNKGNTALHEAVIEKHV-------------FVVELLLLHGASVQ---VLNKRQRTAVDCAEQ 885
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmynFALSLLDKLRDSKElevILNHQGLTPLKLAAK 266


                   ....
gi 116063534   886 NSKI 889
Cdd:TIGR00870  267 EGRI 270
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 788-911 2.12e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  788 GHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGA 867
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 116063534  868 SVQ-VLNKRQRTAVDCAE--QNSKIMELLQVvpscVASLDDVAETDR 911
Cdd:PHA02875   93 FADdVFYKDGMTPLHLATilKKLDIMKLLIA----RGADPDIPNTDK 135
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 2.25e-05

second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the second Zn-fingernail of ANKRD27.


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 42.31  E-value: 2.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 116063534  428 QKMCHPLCFCDDCEKLVSG-RLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22886     3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 733-804 3.28e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  733 SGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLL---------DSNAKP 803
Cdd:PTZ00322  104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKP 183


                  .
gi 116063534  804 N 804
Cdd:PTZ00322  184 D 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
763-817 3.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534   763 LLKHG-ANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYA 817
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-554 3.45e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 3.45e-05
                            10        20
                    ....*....|....*....|....*..
gi 116063534    528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-602 3.91e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 3.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  455 TPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQ---DNNGNT 531
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINnsvDEEGCG 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  532 PLhLACTYGHEDCVKALVYYDVES----------------------------CRLDIGNEK----GDTPLHIAARWGYQG 579
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEArivdkfgknhihrhlmsdnpkastiswmMKLGISPSKpdhdGNTPLHIVCSKTVKN 222

                         170       180
                  ....*....|....*....|....
gi 116063534  580 V-IETLLQNGASTEIQNRLKETPL 602
Cdd:PHA02946  223 VdIINLLLPSTDVNKQNKFGDSPL 246
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-838 4.73e-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: 41.09  E-value: 4.73e-05
                           10        20
                   ....*....|....*....|....*....
gi 116063534   810 GNTPLIYACSGGHHELVALLLQHGASINA 838
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 751-893 4.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  751 AALHGRADLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLL 830
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534  831 QHGASIN-ASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA--EQNSKIMELL 893
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvmMGDIKGIELL 154
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 826-910 5.29e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  826 VALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCAEQNS--KIMELLQVVPSCVASL 903
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQLLSRHSQCHFEL 177


                  ....*..
gi 116063534  904 DDVAETD 910
Cdd:PTZ00322  178 GANAKPD 184
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 456-602 5.33e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  456 PFSRDDRGHTPLHVAAVCG--QASLIdLLVSKGAMVN--ATD--YHGATPLHLACQKgyQSVTLLLLHYKASAEVQdnng 529
Cdd:cd22192    44 LFQRGALGETALHVAALYDnlEAAVV-LMEAAPELVNepMTSdlYQGETALHIAVVN--QNLNLVRELIARGADVV---- 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116063534  530 nTPLhlACTYGHEDCVKALVYYdvescrldignekGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 602
Cdd:cd22192   117 -SPR--ATGTFFRPGPKNLIYY-------------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 6.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.39e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 116063534   456 PFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 8.71e-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: 40.74  E-value: 8.71e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 116063534   564 KGDTPLHIAA-RWGYQGVIETLLQNGASTEIQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-533 1.04e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.33  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116063534  459 RDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPL 533
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 452-527 1.07e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  452 SVVTPF--------SRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAE 523
Cdd:PHA03095  238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317


                  ....
gi 116063534  524 VQDN 527
Cdd:PHA03095  318 TVAA 321
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 842-874 1.97e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 1.97e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 116063534   842 KGNTALHEAVIE-KHVFVVELLLLHGASVQVLNK 874
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
829-883 2.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 116063534   829 LLQHG-ASINASNNKGNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA 883
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 763-839 3.26e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  763 LLKHGANAGARNADQAVPLHLACQQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYaCSGGHHELVA---LLLQHGASINAS 839
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIErinLLVQYGAKINNS 136
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-769 3.53e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.53e-04
                            10        20
                    ....*....|....*....|....*..
gi 116063534    743 DGSSPLHVAALHGRADLIPLLLKHGAN 769
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 786-863 4.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 4.64e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116063534  786 QQGHFQVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 863
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 4.91e-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: 4.91e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 116063534   462 RGHTPLHVAAV-CGQASLIDLLVSKGAMVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 401-560 5.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  401 LFKHIASGNQKEVERLLSQEDHDKDTVQKMCH-PLCFCD-----DCEKLVSGRLNDPSVvtpfSRDDRgHTPLHVAAVCG 474
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMtPLHLATilkklDIMKLLIARGADPDI----PNTDK-FSPLHLAVMMG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  475 QASLIDLLVSKGAMVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGntplhlactyghedCVKALVyYDVE 554
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--------------CVAALC-YAIE 211


                  ....*.
gi 116063534  555 SCRLDI 560
Cdd:PHA02875  212 NNKIDI 217
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 5.42e-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: 5.42e-04
                           10        20
                   ....*....|....*....|....*
gi 116063534   528 NGNTPLHLACT-YGHEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 780-805 6.50e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.50e-04
                            10        20
                    ....*....|....*....|....*.
gi 116063534    780 PLHLACQQGHFQVVKCLLDSNAKPNK 805
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
843-883 7.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.92e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 116063534   843 GNTALHEAVIEKHVFVVELLLLHGASVQVLNKRQRTAVDCA 883
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 780-807 1.06e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....*....
gi 116063534   780 PLHLACQQ-GHFQVVKCLLDSNAKPNKKD 807
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 455-586 1.09e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 42.92  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  455 TPFsRD--DRGHTPLHVAAVCGQASLIDLLVSKGAMVNATD--------------YHGATPLHLA-CQKGYQSVTLLL-- 515
Cdd:cd22195   128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  516 LHYKASAEVQDNNGNTPLH--LACTYGHEDCVKALV-YYDV---------ESCRLD-IGNEKGDTPLHIAARWGYQGVIE 582
Cdd:cd22195   207 AHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGIFQ 286


                  ....
gi 116063534  583 TLLQ 586
Cdd:cd22195   287 HIIR 290
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-554 1.13e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.13e-03
                           10        20
                   ....*....|....*....|....*..
gi 116063534   528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02946 PHA02946
ankyin-like protein; Provisional
 791-869 1.21e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  791 QVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALH------EAVIEKhvfvVELLLL 864
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtdDEVIER----INLLVQ 128


                  ....*
gi 116063534  865 HGASV 869
Cdd:PHA02946  129 YGAKI 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 791-893 1.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  791 QVVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINASNNKGNTALHEAVIEKHVF-----VVELLLLH 865
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 116063534  866 GASVQVLNKRQRTAVDCA----EQNSKIMELL 893
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAiskkSNSYSIVEYL 127
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 711-749 1.33e-03

first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar proteins; ANKRD27, also called VPS9 domain-containing protein, or VARP, is a multifunctional endosomal protein that acts as a regulatory/accessory factor for retromer-based coats. It may be a guanine exchange factor (GEF) for Rab21, Rab32 and Rab38 and may regulate endosome dynamics. It may also regulate the participation of VAMP7 in membrane fusion events and is involved in peripheral melanosomal distribution of TYRP1 in melanocytes. In addition, ANKRD27 participates in GLUT1 endosome-to-plasma membrane trafficking in a VPS29-dependent manner. ANKRD27 contains two conserved CHPLCxCxxC motifs which are referred to as Zn-fingernails. This model corresponds to the first Zn-fingernail of ANKRD27.


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 37.23  E-value: 1.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 116063534  711 CHPLCQCPKCapaQKRLAKVPASGLGVNVTSQD--GSSPLH 749
Cdd:cd22885     3 CHPLCSCDKC---EKLLSGNRNDPSAVTVYSRDdrGYTALH 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-774 1.46e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.46e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 116063534   743 DGSSPLHVAALH-GRADLIPLLLKHGANAGARN 774
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-593 1.47e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.47e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 116063534    564 KGDTPLHIAARWGYQGVIETLLQNGASTEI 593
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-777 2.08e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  559 DIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSK---ILSVMeaYHLsferrqksseAPVQSP 635
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHF----------ASISDP 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  636 QRSVDSisqesstssfssmsassrqeetkkdyrevekLLRAVADGDLEMVRYLLEwteedledaedtvsaadpefchplc 715
Cdd:PLN03192  620 HAAGDL-------------------------------LCTAAKRNDLTAMKELLK------------------------- 643

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116063534  716 qcpkcapaqkrlakvpaSGLGVNVTSQDGSSPLHVAALHGRADLIPLLLKHGANAGARNADQ 777
Cdd:PLN03192  644 -----------------QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 842-869 2.18e-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: 2.18e-03
                            10        20
                    ....*....|....*....|....*...
gi 116063534    842 KGNTALHEAVIEKHVFVVELLLLHGASV 869
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-769 2.27e-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: 36.47  E-value: 2.27e-03
                           10        20
                   ....*....|....*....|....*..
gi 116063534   743 DGSSPLHVAALHGRADLIPLLLKHGAN 769
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 2.51e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.51e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 116063534   565 GDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 3.10e-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: 3.10e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 116063534    462 RGHTPLHVAAVCGQASLIDLLVSKGAMVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
555-602 3.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 116063534   555 SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 602
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
 431-587 3.83e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 3.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  431 CHPLCFCDDCEKLVSGRLN----DPSVVTPFSRDdrgHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLACQK 506
Cdd:PHA02946  142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  507 GYQSVTLL-LLHYKASAEVQDNNGNTPLHL---ACTYGH-------------EDCVKALVYYDVESCrLDIGNEKG---- 565
Cdd:PHA02946  219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTLlikTLSPAHlinkllstsnvitDQTVNICIFYDRDDV-LEIINDKGkqyd 297

                         170       180
                  ....*....|....*....|..
gi 116063534  566 DTPLHIAARWGYQGVIETLLQN 587
Cdd:PHA02946  298 STDFKMAVEVGSIRCVKYLLDN 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-616 4.15e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 4.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 116063534   569 LHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEA 616
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 713-867 5.01e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  713 PLCQCPKCAPAQKRLAKVPAsglgvnvTSQ--DGSSPLHVAALHGRADLIPLLLKHGANAGARNADQAVPLHlACQQGHF 790
Cdd:cd21882    47 LLLEAAPDSGNPKELVNAPC-------TDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRKS-PGNLFYF 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  791 qvvkclldsnakpnkkdlsGNTPLIYACSGGHHELVALLLQHG---ASINASNNKGNTALHEAV------IEKHVFVVE- 860
Cdd:cd21882   119 -------------------GELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVlqadntPENSAFVCQm 179


                  ....*....
gi 116063534  861 --LLLLHGA 867
Cdd:cd21882   180 ynLLLSYGA 188
PHA02946 PHA02946
ankyin-like protein; Provisional
 704-814 6.58e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 6.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  704 SAADPEFCHPLCQCPKcaPAQKRLAKVPASGLGVNVTSQDGSSPLH--VAALHGRADLIPLLLKHGANAGARNADQAVPL 781
Cdd:PHA02946  135 NSVDEEGCGPLLACTD--PSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPL 212

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 116063534  782 HLACQQ--GHFQVVKCLLDSnAKPNKKDLSGNTPL 814
Cdd:PHA02946  213 HIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 792-883 7.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  792 VVKCLLDSNAKPNKKDLSGNTPLIYACSGGHHELVALLLQHGASINA-SNNKGNTALHEAVIEKHVFVVELLLLHGASVQ 870
Cdd:PHA02884   52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADIN 131

                          90
                  ....*....|...
gi 116063534  871 VLNKRQRTAVDCA 883
Cdd:PHA02884  132 IQTNDMVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 454-536 9.91e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 9.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116063534  454 VTPFSR-----------DDRGHTPLHVAAVCGQA----SLIDLLVSKGAMVNATD-YHGATPLHLAC-QKGYQSVTLLLL 516
Cdd:PHA02741   40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCC 119

                          90       100
                  ....*....|....*....|
gi 116063534  517 HYKASAEVQDNNGNTPLHLA 536
Cdd:PHA02741  120 QPGIDLHFCNADNKSPFELA 139
 
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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