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Conserved domains on  [gi|1622898464|ref|XP_028695870|]
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ankyrin repeat domain-containing protein 27 isoform X2 [Macaca mulatta]

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];
717-879 1.65e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 796
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  797 TPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKI 874
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEI 234


                   ....*
gi 1622898464  875 MELLQ 879
Cdd:COG0666    235 VKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.21e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 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 4.70e-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: 83.84  E-value: 4.70e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622898464  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 691-732 1.96e-17

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: 76.59  E-value: 1.96e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622898464  691 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 732
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 1.07e-16

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: 76.48  E-value: 1.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1622898464  344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
717-879 1.65e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 796
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  797 TPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKI 874
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEI 234


                   ....*
gi 1622898464  875 MELLQ 879
Cdd:COG0666    235 VKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.21e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
733-825 1.28e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  733 LHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDsNAKPNKKDlSGNTPLIYACSGGHHEVAA 812
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622898464  813 LLLQHGASINASN 825
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 3.93e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 3.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  500 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1622898464  580 VIETLLQNGASTEIQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 719-859 2.23e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 2.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  719 GLGVNVTSQDGSSPLHVAALH--GRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQV------------------V 778
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrV 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  779 KYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 858
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                   .
gi 1622898464  859 K 859
Cdd:PHA03100   256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 4.70e-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: 83.84  E-value: 4.70e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622898464  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 691-732 1.96e-17

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: 76.59  E-value: 1.96e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622898464  691 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 732
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 1.07e-16

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: 76.48  E-value: 1.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1622898464  344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-626 6.71e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  460 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  520 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622898464  597 -LKETPLKCALNSKIL--SIMEAHHL--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 1.72e-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: 61.73  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  371 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDAVqkmchplcfcddceklvsg 446
Cdd:cd22193      1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  447 rlnDPSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQ 509
Cdd:cd22193     62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  510 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 572
Cdd:cd22193    138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                          250
                   ....*....|....
gi 1622898464  573 ARWGYQGVIETLLQ 586
Cdd:cd22193    216 AKMGKIEILKYILQ 229
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 729-833 1.11e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.26  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLkhgaNAGARNADQAV---------PLHLACQQGHFQVVKYLLDSNA------------K 787
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLM----EAAPELVNEPMtsdlyqgetALHIAVVNQNLNLVRELIARGAdvvspratgtffR 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  788 PNKKDLS--GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALH 833
Cdd:cd22192    127 PGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 7.07e-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: 56.63  E-value: 7.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  449 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGATPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  515 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 1622898464  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 1.38e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 48.22  E-value: 1.38e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464   264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1622898464   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 ...
 795-823 3.77e-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: 44.12  E-value: 3.77e-06
                            10        20
                    ....*....|....*....|....*....
gi 1622898464   795 GNTPLIYACSGGHHEVAALLLQHGASINA 823
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-554 3.04e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.04e-05
                            10        20
                    ....*....|....*....|....*..
gi 1622898464   528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 729-874 5.93e-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: 47.00  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKYLLDSnakpnkkdLS-GNTPL-IYACSGg 806
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  807 HHEVAALLLQHGASINASNNKGNTALHEAVIEKHvFVVE----------LLLLHGASAQ-------VLNKRQRTAVDCAE 869
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENE-FKAEyeelscqmynFALSLLDKLRdskelevILNHQGLTPLKLAA 265


                   ....*
gi 1622898464  870 QNSKI 874
Cdd:TIGR00870  266 KEGRI 270
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
717-879 1.65e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 796
Cdd:COG0666     75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  797 TPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQ--NSKI 874
Cdd:COG0666    155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEI 234


                   ....*
gi 1622898464  875 MELLQ 879
Cdd:COG0666    235 VKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
717-874 1.07e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 1.07e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 796
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  797 TPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQNSKI 874
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
460-864 3.39e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 3.39e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  460 DDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTY 539
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  540 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASteiqnrlketplkcalnskilsimeahhl 619
Cdd:COG0666     98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD----------------------------- 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  620 sferrqkaseapvqspqrsvdsisqesstssfssmsagsrqeetkkdyrevryllewteedledaedtvsaadlefchpl 699
Cdd:COG0666        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  700 cqcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVK 779
Cdd:COG0666    146 ----------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  780 YLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNK 859
Cdd:COG0666    204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                   ....*
gi 1622898464  860 RQRTA 864
Cdd:COG0666    284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 2.21e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 2.21e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-878 3.20e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 3.20e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  710 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPN 789
Cdd:COG0666     35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  790 KKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA- 868
Cdd:COG0666    115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAa 194

                          170
                   ....*....|.
gi 1622898464  869 -EQNSKIMELL 878
Cdd:COG0666    195 eNGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.48e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 1.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  539 YGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    196 NGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
457-832 3.14e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 3.14e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  457 FSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:COG0666     48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  537 CTYGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASteiqnrlketplkcalnskilsimea 616
Cdd:COG0666    128 AYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-------------------------- 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  617 hhlsferrqkaseapvqspqrsvdsisqesstssfssmsagsrqeetkkdyrevryllewteedledaedtvsaadlefc 696
Cdd:COG0666        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  697 hplcqcpkcapaqkrlakvpasglgVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ 776
Cdd:COG0666    179 -------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  777 VVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTAL 832
Cdd:COG0666    234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
733-825 1.28e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 1.28e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  733 LHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDsNAKPNKKDlSGNTPLIYACSGGHHEVAA 812
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1622898464  813 LLLQHGASINASN 825
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-878 1.84e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.84e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  710 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPN 789
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  790 KKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA- 868
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161

                          170
                   ....*....|.
gi 1622898464  869 -EQNSKIMELL 878
Cdd:COG0666    162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
766-853 5.79e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 5.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  766 LHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHgASINASNNkGNTALHEAVIEKHVFVVE 845
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                   ....*...
gi 1622898464  846 LLLLHGAS 853
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-595 3.93e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 3.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  500 LHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALvyydVESCRLDIGNEkGDTPLHIAARWGYQG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL----LEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1622898464  580 VIETLLQNGASTEIQN 595
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 719-859 2.23e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 2.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  719 GLGVNVTSQDGSSPLHVAALH--GRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQV------------------V 778
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrV 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  779 KYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 858
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                   .
gi 1622898464  859 K 859
Cdd:PHA03100   256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 4.70e-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: 83.84  E-value: 4.70e-20
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622898464  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 723-857 2.89e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 2.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  723 NVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYA 802
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  803 CSGGHHEVAALLLQHGASINASNNKGN-TALHEAVIEKHVFVVELLLLHGASAQVL 857
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-554 4.02e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  467 LHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEvqDNNGNTPLHLACTYGHEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1622898464  547 ALVYYDVE 554
Cdd:pfam12796   79 LLLEKGAD 86
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 691-732 1.96e-17

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: 76.59  E-value: 1.96e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622898464  691 ADLEFCHPLCQCPKCAPAQKRLAKVPASGLGVNVTSQDGSSP 732
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 1.07e-16

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: 76.48  E-value: 1.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1622898464  344 AKDELGYCLTSFEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 480-859 2.94e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.57  E-value: 2.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  480 DLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVyydveSCRLD 559
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  560 IgnEKGDTPLHIAARwgyQGVIET---LLQNGASTEIQNRLKETPLKCALNSKILSIMEAHHLSFERRQKASEAPVQSPq 636
Cdd:PHA02876   237 I--NKNDLSLLKAIR---NEDLETsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP- 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  637 rsvdsisqesstssfssmsaGSRQEETKKDYREVRYLLEWTEEdledaedtVSAADLEFCHPLCQCPKCAPAQKRLAKVP 716
Cdd:PHA02876   311 --------------------LYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQASTLDRNKDIVITLL 362

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLA-CQQGHFQVVKYLLDSNAKPNKKDLSG 795
Cdd:PHA02876   363 ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDL 442

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  796 NTPLIYACSGG-HHEVAALLLQHGASINASNNKGNTALHEAvIEKHVfVVELLLLHGAS---AQVLNK 859
Cdd:PHA02876   443 STPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAElrdSRVLHK 508
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-626 6.71e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  460 DDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLL------------------LLHYK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  520 ASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdveSCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNR--- 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622898464  597 -LKETPLKCALNSKIL--SIMEAHHL--SFERRQK 626
Cdd:PHA03100   260 yFKDKDLNTITKIKMLkkSIMYMFLLdpGFYKNRK 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 718-848 1.66e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.01  E-value: 1.66e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  718 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNT 797
Cdd:PHA02874   113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  798 PLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVfVVELLL 848
Cdd:PHA02874   193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 3.42e-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: 3.42e-15
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1622898464  429 KMCHPLCFCDDCEKLVSGRLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 717-868 9.88e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 9.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQD-GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSG 795
Cdd:PHA02878   155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898464  796 NTPLIYACSG-GHHEVAALLLQHGASINA-SNNKGNTALHEAVIEKHvfVVELLLLHGASAQVLNKRQRTAVDCA 868
Cdd:PHA02878   235 NTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 459-607 1.06e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 1.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACT 538
Cdd:PHA02874   120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  539 YGHEDCVKALVyydVESCRLDIGNEKGDTPLHIAARWGyQGVIEtLLQNGASTEIQNRLKETPLKCALN 607
Cdd:PHA02874   200 YGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHN-RSAIE-LLINNASINDQDIDGSTPLHHAIN 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 719-918 1.45e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.45e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  719 GLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTP 798
Cdd:PHA02874   147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  799 LIYACSggHHEVAALLLQHGASINASNNKGNTALHEAVIEK-HVFVVELLLLHGASAQVLNKRQRTAVDCAEQNSKIMEL 877
Cdd:PHA02874   227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV 304

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622898464  878 LQ-VVPSCV--ASLDDVAETDRREYVTVKIRKKWNSKLYDLPDE 918
Cdd:PHA02874   305 IKdIIANAVliKEADKLKDSDFLEHIEIKDNKEFSDFIKECNEE 348
Ank_2 pfam12796
Ankyrin repeats (3 copies);
718-792 2.16e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898464  718 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHgANAGARNADQAvPLHLACQQGHFQVVKYLLDSNAKPNKKD 792
Cdd:pfam12796   19 NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT-ALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 718-856 7.50e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.03  E-value: 7.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  718 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNK---KDls 794
Cdd:PHA02875    24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD-- 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898464  795 GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQV 856
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 478-613 1.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  478 LIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTL--LLLHYKASAEVQDNNGNTPLHLACTYGHED--CVKALVYYDV 553
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGV 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  554 E-------------SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSI 613
Cdd:PHA03100   168 DinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 481-852 3.34e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  481 LLVSKGAVVNATDYHGATPLHLACQKGYQSVT---LLLLHYKASAEVQDNNGNTPLHLACTYGH-EDCVKALVYY--DVE 554
Cdd:PHA03095    32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  555 SCrldigNEKGDTPLHIAAR--WGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSImeahhlsferrqkaseapv 632
Cdd:PHA03095   112 AK-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANV------------------- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  633 qspqrsvdsisqesstssfssmsagsrqeETkkdyreVRYLLewteedleDAEDTVSAADLEF---CHPLCQCPKcaPAQ 709
Cdd:PHA03095   168 -----------------------------EL------LRLLI--------DAGADVYAVDDRFrslLHHHLQSFK--PRA 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  710 KRLAKVPASGLGVNVTSQDGSSPLHVAALHG---RVDLIPLLLKhGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNA 786
Cdd:PHA03095   203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  787 KPNKKDLSGNTPLIYACSGGHHE-VAALLLQHGAS--INASNNKGNTALHEAVIEKHVFVVELLLLHGA 852
Cdd:PHA03095   282 DINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSAetVAATLNTASVAGGDIPSDATRLCVAKVVLRGA 350
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 3.89e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 3.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  461 DRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYg 540
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  541 hedcvkaLVYYDVESCRLDIG---NEK----GDTPLHIAARwgYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA03095 PHA03095
ankyrin-like protein; Provisional
 741-867 5.31e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 5.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  741 RVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ---VVKYLLDSNAKPNKKDLSGNTPLI-YACSGGHHEVAALLLQ 816
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  817 HGASINASNNKGNTALHE--AVIEKHVFVVELLLLHGASAQVLNKRQRTAVDC 867
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA03095 PHA03095
ankyrin-like protein; Provisional
 717-896 8.67e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 8.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHV---AALHGRVDLIPLLLKHGANAGARNADQAVPLHL-ACQQGHFQVVKYLLDSNAKPNKKD 792
Cdd:PHA03095    35 AAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKD 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  793 LSGNTPL-IYACSGG-HHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFV--VELLLLHGASAQVLNKRQRTAVDCA 868
Cdd:PHA03095   115 KVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHH 194

                          170       180
                   ....*....|....*....|....*...
gi 1622898464  869 EQNSKIMEllQVVPSCVASLDDVAETDR 896
Cdd:PHA03095   195 LQSFKPRA--RIVRELIRAGCDPAATDM 220
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 761-878 1.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 1.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  761 DQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHH-----EVAALLLQHGASINASNNKGNTALHEA 835
Cdd:PHA03100    34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622898464  836 VIEK--HVFVVELLLLHGASAQVLNKRQRT----AVDCAEQNSKIMELL 878
Cdd:PHA03100   114 ISKKsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 710-859 1.71e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 1.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  710 KRLAKVPASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-----VVKYLLDS 784
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  785 NAKPNKKDLSGNTPLIYACSG--GHHEVAALLLQHGASINASNNKGNTALHEAVIEKHV--FVVELLLLHGASAQVLNK 859
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR 174
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 694-732 2.63e-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: 2.63e-12
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622898464  694 EFCHPLCQCPKCAPAQKRLAKVPaSGLGVNVTSQDGSSP 732
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDP-SGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-608 4.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 4.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  475 QASLIDLLVSKGAVVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYdv 553
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  554 eSCRLDIGNEKGDTPLHIAArwGY---QGVIETLLQNGASTEIQNRLKE-TPLKCALNS 608
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 743-878 4.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 4.58e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  743 DLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASIN 822
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898464  823 ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA-EQNSKIMELL 878
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELL 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 468-559 5.56e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.93  E-value: 5.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  468 HVAAlCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKA 547
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|..
gi 1622898464  548 LVYYDVESCRLD 559
Cdd:PTZ00322   167 LSRHSQCHFELG 178
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 743-894 7.00e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 7.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  743 DLIPLLLKHGA--NAGARNADQAvPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGAS 820
Cdd:PHA02878   148 EITKLLLSYGAdiNMKDRHKGNT-ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  821 INASNNKGNTALHEAVIE-KHVFVVELLLLHGASAQVLNK-RQRTAVDCAEQNSKIMELLQVVPSCVASLDDVAET 894
Cdd:PHA02878   227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKLT 302
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 473-606 9.42e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 9.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  473 CGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYyd 552
Cdd:PHA02874   101 CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-- 178

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  553 vESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02874   179 -KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
742-878 2.04e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  742 VDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASI 821
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  822 NASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA--EQNSKIMELL 878
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayNGNLEIVKLL 139
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 2.36e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKgAVVNATDYhGATPLHLACQKGYQSVTLLLLHYKASAEVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
765-815 4.10e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.10e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  765 PLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLL 815
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-881 4.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.01  E-value: 4.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  567 TPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEAhhlsferrqkaseapvqspqrSVDSisqes 646
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA---------------------IIDN----- 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  647 stssfssmsagsRQEETKKDYREVRYLlewTEEDLE------DAEDTVSAADLEFCHPLCQCPKcAPAQKRLA-KVPASG 719
Cdd:PHA02876   234 ------------RSNINKNDLSLLKAI---RNEDLEtslllyDAGFSVNSIDDCKNTPLHHASQ-APSLSRLVpKLLERG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  720 LGVNVTSQDGSSPLHVAALHG-RVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQ-VVKYLLDSNAKPNKKDLSGNT 797
Cdd:PHA02876   298 ADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKT 377

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  798 PLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFV-VELLLLHGASAQVLNKRQRTAVDCAEQNSKIME 876
Cdd:PHA02876   378 PIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLD 457


                   ....*
gi 1622898464  877 LLQVV 881
Cdd:PHA02876   458 VIEML 462
Ank_4 pfam13637
Ankyrin repeats (many copies);
729-782 5.19e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 5.19e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLL 782
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
795-848 1.23e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.23e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  795 GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 848
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 463-613 1.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  463 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKG-YQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 541
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898464  542 EDCVKALVYYDVEScrlDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSI 613
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 745-817 3.74e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 63.76  E-value: 3.74e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  745 IPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQH 817
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 709-853 4.52e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 4.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  709 QKRLAKVPASGLGVNVTSQDG----SSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDS 784
Cdd:PLN03192   501 HKELHDLNVGDLLGDNGGEHDdpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  785 NAKPNKKDLSGNTPLIYACSGGHHEV-------AAL------------------------LLQHGASINASNNKGNTALH 833
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHHKIfrilyhfASIsdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQ 660

                          170       180
                   ....*....|....*....|
gi 1622898464  834 EAVIEKHVFVVELLLLHGAS 853
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGAD 680
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 466-617 7.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 7.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  466 PLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQ---------------------------------------- 505
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  506 ------KGYQS------------------VTLLLLHYKASAEVQD-NNGNTPLHLACTYGHEDCVKALVYYDVESCRLDI 560
Cdd:PHA02878   120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  561 GNekgDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCA----LNSKILSIMEAH 617
Cdd:PHA02878   200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 465-604 1.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  465 TPLHVAALCGQASLIDLLVSKGAVVNATDYH-GATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHED 543
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  544 CVKALVyyDVESCrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKC 604
Cdd:PHA02875   150 GIELLI--DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 371-586 1.72e-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: 61.73  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  371 PPESEGFGDRLFLKQRMSLLSQMTSSPT--DCLFKHIAS--GNQKEVERLLSQEDHDKDAVqkmchplcfcddceklvsg 446
Cdd:cd22193      1 LEELLGFLQDLCRRRKDLTDSEFTESSTgkTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  447 rlnDPSVVTPFsRDD--RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQ 509
Cdd:cd22193     62 ---KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  510 SVTLLL--LHYKASAEVQDNNGNTPLHLACTYG-----HEDCVKALvyYD---VESCRL-------DIGNEKGDTPLHIA 572
Cdd:cd22193    138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                          250
                   ....*....|....
gi 1622898464  573 ARWGYQGVIETLLQ 586
Cdd:cd22193    216 AKMGKIEILKYILQ 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 722-858 3.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  722 VNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYL-------------------- 781
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmi 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  782 ---LDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLN 858
Cdd:PHA02874   108 ktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-606 3.18e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 3.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  470 AALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 549
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898464  550 YYdvesCRLDIGNEKGDTpLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PLN03192   612 HF----ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 723-874 4.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  723 NVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAG-ARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIY 801
Cdd:PHA02875    62 DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  802 ACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDC-AEQNSKI 874
Cdd:PHA02875   142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
PHA02798 PHA02798
ankyrin-like protein; Provisional
 742-867 4.44e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 4.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  742 VDLIPLLLKHGANAGARNADQAVPL-----HLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGH---HEVAAL 813
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  814 LLQHGASINASNNKGNTALHEAVIEKH---VFVVELLLLHGASA-QVLNKRQRTAVDC 867
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDInTHNNKEKYDTLHC 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 721-896 7.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 7.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  721 GVNVTSQD--GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSgntp 798
Cdd:PHA02876   168 GADVNAKDiyCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  799 LIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVF-VVELLLLHGASAQVLNKRQRTAVDCAEQNSKIMEL 877
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEN 323

                          170
                   ....*....|....*....
gi 1622898464  878 LQVVPSCVAsldDVAETDR 896
Cdd:PHA02876   324 IRTLIMLGA---DVNAADR 339
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-606 8.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 8.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  458 SRDDRGHTPLHVAALCGQAS-LIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTL-LLLHYKASAEVQDNNGNTPLHL 535
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622898464  536 ACTYG-HEDCVKALVYYDVESCRLDIGNEkgdTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02876   348 ASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 729-833 1.11e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.26  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLkhgaNAGARNADQAV---------PLHLACQQGHFQVVKYLLDSNA------------K 787
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLM----EAAPELVNEPMtsdlyqgetALHIAVVNQNLNLVRELIARGAdvvspratgtffR 126

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  788 PNKKDLS--GNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALH 833
Cdd:cd22192    127 PGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA03095 PHA03095
ankyrin-like protein; Provisional
 459-602 1.59e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVAaLCGQ---ASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEV--QDNNGNTPL 533
Cdd:PHA03095   113 KDKVGRTPLHVY-LSGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyaVDDRFRSLL 191

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  534 HLACTYGH--EDCVKALVYYDVE-------------------SCR-------------LDIGNEKGDTPLHIAARWGYQG 579
Cdd:PHA03095   192 HHHLQSFKprARIVRELIRAGCDpaatdmlgntplhsmatgsSCKrslvlplliagisINARNRYGQTPLHYAAVFNNPR 271

                          170       180
                   ....*....|....*....|...
gi 1622898464  580 VIETLLQNGASTEIQNRLKETPL 602
Cdd:PHA03095   272 ACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
498-549 1.65e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.65e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622898464  498 TPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALV 549
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 383-594 1.72e-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: 58.35  E-value: 1.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  383 LKQRMSLLSQMTSSPTDCLFKHIASGNQKEVERLLSQEDHDKDAVQKMCHPLCFCDDCEKLVsgrlNDPSVVTPFsrddR 462
Cdd:cd21882      1 LEELLGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKELV----NAPCTDEFY----Q 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  463 GHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGATPLHL-ACQKGYQSVTLLLLH--YKASAEVQD 526
Cdd:cd21882     73 GQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  527 NNGNTPLH--------------LACTYGHEdcvkaLVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGVIETLLQNG 588
Cdd:cd21882    153 SLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227


                   ....*.
gi 1622898464  589 ASTEIQ 594
Cdd:cd21882    228 FSGPYQ 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 717-822 1.78e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  717 ASGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGN 796
Cdd:PHA02875   123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                           90       100
                   ....*....|....*....|....*..
gi 1622898464  797 -TPLIYACSGGHHEVAALLLQHGASIN 822
Cdd:PHA02875   203 vAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 2.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 2.26e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  482 LVSKGAV-VNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 456-547 3.91e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  456 PFSRDDRGHTPLHVAALCG--QASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPL 533
Cdd:PHA03095   215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                           90
                   ....*....|....
gi 1622898464  534 HLACTYGHEDCVKA 547
Cdd:PHA03095   295 SLMVRNNNGRAVRA 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 4.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 4.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  461 DRGHTPLHVAALCGQaSLIDLLVSKgAVVNATDYHGATPLHLA----CQKgyqSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:PHA02874   221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                   ....*....
gi 1622898464  537 CTYGHEDCV 545
Cdd:PHA02874   296 FKYINKDPV 304
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 465-606 5.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 5.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  465 TPLHvaalcgQASLID-------LLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLA- 536
Cdd:PHA02876   343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  537 CTYGHEDCVKALVYydvESCRLDIGNEKGDTPLHIAARWGYQ-GVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:PHA02876   417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 732-878 6.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 6.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  732 PLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAK------------------------ 787
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfytlvaikdafnnrnveifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  788 --PNKKDLSGNTPLIYACSGGHH-----EVAALLLQHGASIN-ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNK 859
Cdd:PHA02878   120 ilTNRYKNIQTIDLVYIDKKSKDdiieaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                          170       180
                   ....*....|....*....|.
gi 1622898464  860 RQRTAVDCA--EQNSKIMELL 878
Cdd:PHA02878   200 TNNSPLHHAvkHYNKPIVHIL 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 449-586 7.07e-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: 56.63  E-value: 7.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  449 NDPSvvtpFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNA------------TD--YHGATPLHLACQKGYQSVTLL 514
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  515 LLHYKASAEVQDNNGNTPLHLAC----------TYGHEdCVKALVYYDVESCRL----DIGNEKGDTPLHIAARWGYQGV 580
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 1622898464  581 IETLLQ 586
Cdd:TIGR00870  273 FRLKLA 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-549 1.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGH 541
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                   ....*...
gi 1622898464  542 EDCVKALV 549
Cdd:PHA02875   181 IAICKMLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 778-850 1.67e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.67e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  778 VKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLH 850
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 2.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  459 RDDRGHTPLHVA-ALCGQASLIDLLVSKGAVVNATDY-HGATPLHLACQKgyQSVTLLLLHYKASAEVQDNNGNTPLHLA 536
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                           90       100
                   ....*....|....*....|....*.
gi 1622898464  537 ctyghedcvkALVYYDVESCRLDIGN 562
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 3.55e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 3.55e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  514 LLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVEscrLDIGNEKGDTPLHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 3.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.73e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622898464  529 GNTPLHLACTYGHEDCVKALVYYDVESCRLDIGnekGDTPLHIAARWGYQGVIETLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
788-835 4.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 4.37e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  788 PNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEA 835
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 467-615 5.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  467 LHVAALC-----GQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGh 541
Cdd:PHA02875     1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG- 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  542 eDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIME 615
Cdd:PHA02875    80 -DVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
Ank_5 pfam13857
Ankyrin repeats (many copies);
748-802 1.10e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 1.10e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  748 LLKHG-ANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYA 802
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 795-826 1.32e-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: 45.74  E-value: 1.32e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622898464  795 GNTPLIYAC-SGGHHEVAALLLQHGASINASNN 826
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 1.38e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 48.22  E-value: 1.38e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464   264 IPRAKRELAQLNKCTSPQQKLVCLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1622898464   344 AKDELGYCLTSFEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 1.75e-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: 51.94  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  463 GHTPLHVAALCGQASLIDLLVSKGAVVN---ATD-----------YHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 528
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622898464  529 GNTPLH---------LAC-TYgheDCVKALVYYDVESCRLDIGNEKGDTPLHIAARWGYQGVIETLLQN 587
Cdd:cd22192    169 GNTVLHilvlqpnktFACqMY---DLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 456-518 1.98e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.98e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHY 518
Cdd:PTZ00322   108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 781-854 2.31e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 2.31e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  781 LLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVElLLLHGASA 854
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASI 616
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 3.06e-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: 3.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD-------------YHGATPLHL-ACQKGYQSVTLLL--LHYKASAEVQ 525
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622898464  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 3.44e-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: 50.91  E-value: 3.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQSVTLLLLHYKASAEVQD 526
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  527 NNGNTPLHLACTYG-----HEDCVKALvyYDV-----ESCRLD-IGNEKGDTPLHIAARWG 576
Cdd:cd22194    220 SRGNTVLHALVTVAedsktQNDFVKRM--YDMillksENKNLEtIRNNEGLTPLQLAAKMG 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 773-896 3.69e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 3.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  773 GHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGA 852
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1622898464  853 SAQ-VLNKRQRTAVDCAE--QNSKIMELLQVvpscVASLDDVAETDR 896
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATilKKLDIMKLLIA----RGADPDIPNTDK 135
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 795-823 3.77e-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: 44.12  E-value: 3.77e-06
                            10        20
                    ....*....|....*....|....*....
gi 1622898464   795 GNTPLIYACSGGHHEVAALLLQHGASINA 823
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
722-769 4.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.51e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  722 VNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLA 769
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
463-516 5.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622898464  463 GHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLL 516
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 718-789 8.05e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 8.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  718 SGLGVNVTSQDGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLL---------DSNAKP 788
Cdd:PTZ00322   104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKP 183


                   .
gi 1622898464  789 N 789
Cdd:PTZ00322   184 D 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 458-528 9.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 9.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622898464  458 SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNN 528
Cdd:PHA03100   187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 460-595 1.07e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  460 DDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQdnNGNTPLHLACTY 539
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKR 632

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  540 GHEDCVKALVYYDVEscrLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQN 595
Cdd:PLN03192   633 NDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 462-595 1.53e-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: 49.03  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  462 RGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHL-ACQKGYQSVTLLLL--HYKASAEV 524
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  525 QDNNGNTPLHLACTYG--------------HEDCVKALVYYDVESCRlDIGNEKGDTPLHIAARWGYQGVIETLLQNgas 590
Cdd:cd22196    173 RDSMGNTVLHALVEVAdntpentkfvtkmyNEILILGAKIRPLLKLE-EITNKKGLTPLKLAAKTGKIGIFAYILGR--- 248


                   ....*
gi 1622898464  591 tEIQN 595
Cdd:cd22196    249 -EIKE 252
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 1.62e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  456 PFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 456-602 1.63e-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: 48.86  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  456 PFSRDDRGHTPLHVAALCG--QASLIdLLVSKGAVVN--ATD--YHGATPLHLACQKgyQSVTLLLLHYKASAEVQdnng 529
Cdd:cd22192     44 LFQRGALGETALHVAALYDnlEAAVV-LMEAAPELVNepMTSdlYQGETALHIAVVN--QNLNLVRELIARGADVV---- 116

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  530 nTPLhlACTYGHEDCVKALVYYdvescrldignekGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 602
Cdd:cd22192    117 -SPR--ATGTFFRPGPKNLIYY-------------GEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 1.78e-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: 42.70  E-value: 1.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622898464  428 QKMCHPLCFCDDCEKLVSG-RLNDPSVVTPFSRDDRGHTP 466
Cdd:cd22886      3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-554 3.04e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.04e-05
                            10        20
                    ....*....|....*....|....*..
gi 1622898464   528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-602 3.54e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  455 TPFSRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQ---DNNGNT 531
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYGAKINnsvDEEGCG 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  532 PLhLACTYGHEDCVKALVYYDVES----------------------------CRLDIGNEK----GDTPLHIAARWGYQG 579
Cdd:PHA02946   144 PL-LACTDPSERVFKKIMSIGFEArivdkfgknhihrhlmsdnpkastiswmMKLGISPSKpdhdGNTPLHIVCSKTVKN 222

                          170       180
                   ....*....|....*....|....
gi 1622898464  580 V-IETLLQNGASTEIQNRLKETPL 602
Cdd:PHA02946   223 VdIINLLLPSTDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 811-895 5.22e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  811 AALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCAEQNS--KIMELLQVVPSCVASL 888
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQLLSRHSQCHFEL 177


                   ....*..
gi 1622898464  889 DDVAETD 895
Cdd:PTZ00322   178 GANAKPD 184
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 729-874 5.93e-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: 47.00  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLKHGANAGARnadqavplhlACqqGHFQVVKYLLDSnakpnkkdLS-GNTPL-IYACSGg 806
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPAR----------AC--GDFFVKSQGVDS--------FYhGESPLnAAACLG- 186

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  807 HHEVAALLLQHGASINASNNKGNTALHEAVIEKHvFVVE----------LLLLHGASAQ-------VLNKRQRTAVDCAE 869
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLHLLVMENE-FKAEyeelscqmynFALSLLDKLRdskelevILNHQGLTPLKLAA 265


                   ....*
gi 1622898464  870 QNSKI 874
Cdd:TIGR00870  266 KEGRI 270
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 736-878 7.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 7.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  736 AALHGRVDLIPLLLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLL 815
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  816 QHGASIN-ASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA--EQNSKIMELL 878
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvmMGDIKGIELL 154
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 7.83e-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: 7.83e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622898464  564 KGDTPLHIAA-RWGYQGVIETLLQNGASTEIQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 795-823 1.44e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 1.44e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622898464  795 GNTPLIYACSGGHHEVAALLLQHGASINA 823
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 765-792 1.73e-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: 1.73e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622898464  765 PLHLACQQ-GHFQVVKYLLDSNAKPNKKD 792
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
814-868 1.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.87e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622898464  814 LLQHG-ASINASNNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA 868
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 728-754 2.02e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.02e-04
                            10        20
                    ....*....|....*....|....*..
gi 1622898464   728 DGSSPLHVAALHGRVDLIPLLLKHGAN 754
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA03095 PHA03095
ankyrin-like protein; Provisional
 456-540 2.20e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  456 PFSRDDRGHTPLHVAALC--GQASLIDLLVSKGAVVNATDYHGATPLHLACQKG--YQSVTLLLLHYKASAEVQDNNGNT 531
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQT 259


                   ....*....
gi 1622898464  532 PLHLACTYG 540
Cdd:PHA03095   260 PLHYAAVFN 268
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 765-790 2.59e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.59e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622898464   765 PLHLACQQGHFQVVKYLLDSNAKPNK 790
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 2.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.75e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622898464  462 RGHTPLHVAAL-CGQASLIDLLVSKGAVVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 748-859 2.78e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  748 LLKHGANAGARNADQAVPLHLACQQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYaCSGGHHEVAA---LLLQHGASINAS 824
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIErinLLVQYGAKINNS 136

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1622898464  825 NNKGNTALHEAVIEKHVFVVELLLLHGASAQVLNK 859
Cdd:PHA02946   137 VDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDK 171
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 401-560 2.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  401 LFKHIASGNQKEVERLLSQEDHDKDAVQKMCH-PLCFCD-----DCEKLVSGRLNDPSVvtpfSRDDRgHTPLHVAALCG 474
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMtPLHLATilkklDIMKLLIARGADPDI----PNTDK-FSPLHLAVMMG 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  475 QASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAEVQDNNGntplhlactyghedCVKALVyYDVE 554
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--------------CVAALC-YAIE 211


                   ....*.
gi 1622898464  555 SCRLDI 560
Cdd:PHA02875   212 NNKIDI 217
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 4.92e-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: 4.92e-04
                           10        20
                   ....*....|....*....|....*
gi 1622898464  528 NGNTPLHLACT-YGHEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
PHA03095 PHA03095
ankyrin-like protein; Provisional
 452-527 5.08e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  452 SVVTPF--------SRDDRGHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQKGYQSVTLLLLHYKASAE 523
Cdd:PHA03095   238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317


                   ....
gi 1622898464  524 VQDN 527
Cdd:PHA03095   318 TVAA 321
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 728-759 6.60e-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: 38.04  E-value: 6.60e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622898464  728 DGSSPLHVAALH-GRVDLIPLLLKHGANAGARN 759
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 6.77e-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: 6.77e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622898464   462 RGHTPLHVAALCGQASLIDLLVSKGAVVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 728-754 7.05e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 7.05e-04
                           10        20
                   ....*....|....*....|....*..
gi 1622898464  728 DGSSPLHVAALHGRVDLIPLLLKHGAN 754
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-554 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622898464  528 NGNTPLHLACTYGHEDCVKALVYYDVE 554
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 696-734 1.13e-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: 37.62  E-value: 1.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622898464  696 CHPLCQCPKCapaQKRLAKVPASGLGVNVTSQD--GSSPLH 734
Cdd:cd22885      3 CHPLCSCDKC---EKLLSGNRNDPSAVTVYSRDdrGYTALH 40
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 455-586 1.24e-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: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  455 TPFsRD--DRGHTPLHVAALCGQASLIDLLVSKGAVVNATD--------------YHGATPLHLA-CQKGYQSVTLLL-- 515
Cdd:cd22195    128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  516 LHYKASAEVQDNNGNTPLH--LACTYGHEDCVKALV-YYDV---------ESCRLD-IGNEKGDTPLHIAARWGYQGVIE 582
Cdd:cd22195    207 AHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGIFQ 286


                   ....
gi 1622898464  583 TLLQ 586
Cdd:cd22195    287 HIIR 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-593 1.33e-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: 37.18  E-value: 1.33e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1622898464   564 KGDTPLHIAARWGYQGVIETLLQNGASTEI 593
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 776-878 1.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  776 QVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVF-----VVELLLLH 850
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622898464  851 GASAQVLNKRQRTAVDCA----EQNSKIMELL 878
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAiskkSNSYSIVEYL 127
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 827-859 1.77e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1622898464  827 KGNTALHEAVIE-KHVFVVELLLLHGASAQVLNK 859
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-616 1.88e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  569 LHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSIMEA 616
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 453-589 2.08e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  453 VVTPFSRDDRGHTPLHVaaLCGQASLIDLLVSKGAVVNATDY-------HGATPLHLACQKGY---QSVTLLLLHYKASA 522
Cdd:PHA02736     7 IIFASEPDIEGENILHY--LCRNGGVTDLLAFKNAISDENRYlvleynrHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622898464  523 EVQDN-NGNTPLHLACTYGHEDCVKALvyydvesCR-----LDIGNEKGDTPLHIAARWGYQGVIETLLQNGA 589
Cdd:PHA02736    85 NGKERvFGNTPLHIAVYTQNYELATWL-------CNqpgvnMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 771-848 2.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 2.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622898464  771 QQGHFQVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALHEAVIEKHVFVVELLL 848
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
828-868 2.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622898464  828 GNTALHEAVIEKHVFVVELLLLHGASAQVLNKRQRTAVDCA 868
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 765-790 2.32e-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: 2.32e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622898464  765 PLHLACQQGHFQVVKYLLDSNAKPNK 790
Cdd:pfam13606    5 PLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 2.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622898464  565 GDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-613 2.78e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 2.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622898464  559 DIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSI 613
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
PHA02946 PHA02946
ankyin-like protein; Provisional
 776-852 3.18e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  776 QVVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINASNNKGNTALH------EAVIEKhvfvVELLLL 849
Cdd:PHA02946    53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylsgtdDEVIER----INLLVQ 128


                   ...
gi 1622898464  850 HGA 852
Cdd:PHA02946   129 YGA 131
Ank_5 pfam13857
Ankyrin repeats (many copies);
555-602 3.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.25e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622898464  555 SCRLDIGNEKGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPL 602
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
 431-587 3.81e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 3.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  431 CHPLCFCDDCEKLVSGRLN----DPSVVTPFSRDdrgHTPLHVAALCGQASLIDLLVSKGAVVNATDYHGATPLHLACQK 506
Cdd:PHA02946   142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  507 GYQSVTLL-LLHYKASAEVQDNNGNTPLHL---ACTYGH-------------EDCVKALVYYDVESCrLDIGNEKG---- 565
Cdd:PHA02946   219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTLlikTLSPAHlinkllstsnvitDQTVNICIFYDRDDV-LEIINDKGkqyd 297

                          170       180
                   ....*....|....*....|..
gi 1622898464  566 DTPLHIAARWGYQGVIETLLQN 587
Cdd:PHA02946   298 STDFKMAVEVGSIRCVKYLLDN 319
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 827-853 5.03e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 5.03e-03
                            10        20
                    ....*....|....*....|....*..
gi 1622898464   827 KGNTALHEAVIEKHVFVVELLLLHGAS 853
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 729-832 5.41e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.61  E-value: 5.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  729 GSSPLHVAALHGRVDLIPLLLKHGANAGARNADQ-------------AVPLHLACQQGHFQVVKYLLDSNAKP---NKKD 792
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQD 173

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1622898464  793 LSGNTPLiyacsgghhevaalllqHGASINASNNKGNTAL 832
Cdd:cd22197    174 SLGNTVL-----------------HALVMIADNSPENSAL 196
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 693-852 7.14e-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: 40.25  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  693 LEFCHPLCQCPKCAPAQKRLAKVPAsglgvnvTSQ--DGSSPLHVAALHGRVDLIPLLLKHGANAGARNADQAVPLHlAC 770
Cdd:cd21882     42 NEAIMLLLEAAPDSGNPKELVNAPC-------TDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFFRKS-PG 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  771 QQGHFqvvkylldsnakpnkkdlsGNTPLIYACSGGHHEVAALLLQHG---ASINASNNKGNTALHEAV------IEKHV 841
Cdd:cd21882    114 NLFYF-------------------GELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHALVlqadntPENSA 174

                          170
                   ....*....|....
gi 1622898464  842 FVVE---LLLLHGA 852
Cdd:cd21882    175 FVCQmynLLLSYGA 188
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 718-828 7.75e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  718 SGLGVN-VTSQDGSSPLHVAALHGR---VDLIPLLLKHGANAGARNADQAVPLH--LACQQGHFQVVKYLLDSNAKPNKK 791
Cdd:PHA02859    75 NGADVNfKTRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNK 154

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1622898464  792 DLSGNTPL-IYACSGGHHEVAALLLQHGASINASNNKG 828
Cdd:PHA02859   155 DFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSG 192
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 777-868 8.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622898464  777 VVKYLLDSNAKPNKKDLSGNTPLIYACSGGHHEVAALLLQHGASINA-SNNKGNTALHEAVIEKHVFVVELLLLHGASAQ 855
Cdd:PHA02884    52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGADIN 131

                           90
                   ....*....|...
gi 1622898464  856 VLNKRQRTAVDCA 868
Cdd:PHA02884   132 IQTNDMVTPIELA 144
 
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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