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Conserved domains on  [gi|1953273547|ref|XP_038513549|]
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ankyrin repeat domain-containing protein 27 isoform X5 [Canis lupus familiaris]

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];
789-1048 6.11e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 6.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  789 LLRAVADGDLEMVRYLLEWTEEDLDELEDAAAVGDVDFCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSPLHVAA 868
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  869 LHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQH 948
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  949 GASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCAEQ--NSKIMELLQVVPSCVASVDDVGQTD 1026
Cdd:COG0666    176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                          250       260
                   ....*....|....*....|..
gi 1953273547 1027 RKEYVTVKIRKKWNSKMYDLPD 1048
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-732 1.66e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 1.66e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  655 YGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEA 732
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 545-584 3.75e-19

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: 81.53  E-value: 3.75e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1953273547  545 RMCHPLCFCDDCEKLVSGRLNDPSIVTPFSRDDRGHTPLH 584
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 380-479 8.04e-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: 74.17  E-value: 8.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  380 IPRAKRELAQLNKCTSPQQKLICLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 459
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1953273547  460 AKDELGYCLTSIEAAIEYIR 479
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
789-1048 6.11e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 6.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  789 LLRAVADGDLEMVRYLLEWTEEDLDELEDAAAVGDVDFCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSPLHVAA 868
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  869 LHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQH 948
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  949 GASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCAEQ--NSKIMELLQVVPSCVASVDDVGQTD 1026
Cdd:COG0666    176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                          250       260
                   ....*....|....*....|..
gi 1953273547 1027 RKEYVTVKIRKKWNSKMYDLPD 1048
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-732 1.66e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 1.66e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  655 YGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEA 732
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
864-954 4.13e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 4.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  864 LHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDsKAKPNKKDiSGNTPLIYACSNGYHEVAA 943
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1953273547  944 LLLQHGASINI 954
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
616-711 1.18e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  616 LHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYDVQSCRLDignekGDTPLHIAARWGYQG 695
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1953273547  696 IIETLLQNGASTEIQN 711
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 850-990 3.54e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.51  E-value: 3.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALH--GRADLIPLLLKHGANAGARNVNQAVPLHLA--CQKGHFQVVRCLLDSKAKPNKK--- 922
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrv 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  923 -------------DISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVN 989
Cdd:PHA03100   176 nyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                   .
gi 1953273547  990 K 990
Cdd:PHA03100   256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 545-584 3.75e-19

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: 81.53  E-value: 3.75e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1953273547  545 RMCHPLCFCDDCEKLVSGRLNDPSIVTPFSRDDRGHTPLH 584
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 822-863 5.01e-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: 75.44  E-value: 5.01e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1953273547  822 GDVDFCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSP 863
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 576-735 8.44e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 8.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  576 DDRGHTPLHVAALC--GQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLL------------------LLHYK 635
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  636 ASPEVQDNNGNTPLHLACAYGHEDCVKALVYYdvqSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNR--- 712
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                          170       180
                   ....*....|....*....|....*.
gi 1953273547  713 -LKETPLNCALNSKIL--SIMEAHHL 735
Cdd:PHA03100   260 yFKDKDLNTITKIKMLkkSIMYMFLL 285
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 380-479 8.04e-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: 74.17  E-value: 8.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  380 IPRAKRELAQLNKCTSPQQKLICLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 459
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1953273547  460 AKDELGYCLTSIEAAIEYIR 479
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 565-702 4.55e-09

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: 60.48  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  565 NDPSivtpFSRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNA------------TD--YHGSAPLHLACQKGYQSVTLL 630
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  631 LLHYKASPEVQDNNGNTPLHLAC----------AYGHEdCVKALVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGI 696
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 1953273547  697 IETLLQ 702
Cdd:TIGR00870  273 FRLKLA 278
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 578-710 1.33e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.12  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATD-------------YHGSAPLHL-ACQKGYQSVTLLLLH--YKASPEVQ 641
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQ 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  642 DNNGNTPLH--------------LACAYGHEdcvkaLVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGIIETLLQN 703
Cdd:cd21882    152 DSLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226


                   ....*..
gi 1953273547  704 GASTEIQ 710
Cdd:cd21882    227 EFSGPYQ 233
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 380-478 1.93e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 47.84  E-value: 1.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547   380 IPRAKRELAQLNKCTSPQQKLICLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 459
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1953273547   460 AKDELGYCLTSIEAAIEYI 478
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 926-954 3.45e-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: 44.50  E-value: 3.45e-06
                            10        20
                    ....*....|....*....|....*....
gi 1953273547   926 GNTPLIYACSNGYHEVAALLLQHGASINI 954
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 644-669 2.08e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.08e-05
                            10        20
                    ....*....|....*....|....*.
gi 1953273547   644 NGNTPLHLACAYGHEDCVKALVYYDV 669
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 860-970 1.44e-03

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: 42.76  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  860 GTSPLHVAALHGRADLIPLLLKHGANAGAR-NVNqavplhlACQKGhfQVVRCLLDSKAKPNkkdisgntplIYACSnGY 938
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARaCGD-------FFVKS--QGVDSFYHGESPLN----------AAACL-GS 187

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1953273547  939 HEVAALLLQHGASINICNNKGNTALHEAVIEK 970
Cdd:TIGR00870  188 PSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
789-1048 6.11e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 6.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  789 LLRAVADGDLEMVRYLLEWTEEDLDELEDAAAVGDVDFCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSPLHVAA 868
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  869 LHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQH 948
Cdd:COG0666     96 RNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  949 GASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCAEQ--NSKIMELLQVVPSCVASVDDVGQTD 1026
Cdd:COG0666    176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAEngNLEIVKLLLEAGADLNAKDKDGLTA 255

                          250       260
                   ....*....|....*....|..
gi 1953273547 1027 RKEYVTVKIRKKWNSKMYDLPD 1048
Cdd:COG0666    256 LLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
592-983 1.20e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 1.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  592 ASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYDVqs 671
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  672 cRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPlncalnskilsimeahhlplerrrkssevpvqpp 751
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP---------------------------------- 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  752 qrpadsisqasstssfssvlassrqeepkkdyrevekLLRAVADGDLEMVRYLLEwteedldeledaaavgdvdfchplc 831
Cdd:COG0666    124 -------------------------------------LHLAAYNGNLEIVKLLLE------------------------- 141

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  832 qcprcapaqkklakipaSGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRC 911
Cdd:COG0666    142 -----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953273547  912 LLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGA 983
Cdd:COG0666    205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-732 1.66e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 1.66e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  655 YGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEA 732
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-732 2.97e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 2.97e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  655 YGHEDCVKALVYYDVqscRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEA 732
Cdd:COG0666    196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
841-1009 2.37e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 2.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  841 KKLAKIPASGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPN 920
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  921 KKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA- 999
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161

                          170
                   ....*....|.
gi 1953273547 1000 -EQNSKIMELL 1009
Cdd:COG0666    162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
864-954 4.13e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 4.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  864 LHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDsKAKPNKKDiSGNTPLIYACSNGYHEVAA 943
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1953273547  944 LLLQHGASINI 954
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
897-989 6.40e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.03  E-value: 6.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  897 LHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHgASINICNNkGNTALHEAVIEKHVFVVE 976
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1953273547  977 LLLLHGASVQVVN 989
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
616-711 1.18e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.18e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  616 LHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYDVQSCRLDignekGDTPLHIAARWGYQG 695
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-----GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1953273547  696 IIETLLQNGASTEIQN 711
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 850-990 3.54e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.51  E-value: 3.54e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALH--GRADLIPLLLKHGANAGARNVNQAVPLHLA--CQKGHFQVVRCLLDSKAKPNKK--- 922
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKnrv 175

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  923 -------------DISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVN 989
Cdd:PHA03100   176 nyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255


                   .
gi 1953273547  990 K 990
Cdd:PHA03100   256 E 256
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 545-584 3.75e-19

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: 81.53  E-value: 3.75e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1953273547  545 RMCHPLCFCDDCEKLVSGRLNDPSIVTPFSRDDRGHTPLH 584
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 814-997 1.40e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.58  E-value: 1.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  814 ELEDAAAVGDVdfchplcqcprcapaqKKLAKIPASGLGVN-VTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVN 892
Cdd:PHA02875    71 ELHDAVEEGDV----------------KAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  893 QAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGN-TALHEAVIEKH 971
Cdd:PHA02875   135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNK 214

                          170       180
                   ....*....|....*....|....*....
gi 1953273547  972 VFVVELLLLHGAS---VQVVNKRQCTAID 997
Cdd:PHA02875   215 IDIVRLFIKRGADcniMFMIEGEECTILD 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
583-669 4.51e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 4.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  583 LHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLhYKASPEVQDnNGNTPLHLACAYGHEDCVK 662
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1953273547  663 ALVYYDV 669
Cdd:pfam12796   79 LLLEKGA 85
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 822-863 5.01e-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: 75.44  E-value: 5.01e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1953273547  822 GDVDFCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSP 863
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 576-735 8.44e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 8.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  576 DDRGHTPLHVAALC--GQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLL------------------LLHYK 635
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILkllidkgvdinaknrvnyLLSYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  636 ASPEVQDNNGNTPLHLACAYGHEDCVKALVYYdvqSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNR--- 712
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL---GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEtll 259

                          170       180
                   ....*....|....*....|....*.
gi 1953273547  713 -LKETPLNCALNSKIL--SIMEAHHL 735
Cdd:PHA03100   260 yFKDKDLNTITKIKMLkkSIMYMFLL 285
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 846-979 7.91e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 7.91e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  846 IPASGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDIS 925
Cdd:PHA02874   110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  926 GNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVfVVELLL 979
Cdd:PHA02874   190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLI 242
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 380-479 8.04e-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: 74.17  E-value: 8.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  380 IPRAKRELAQLNKCTSPQQKLICLRKVVQLITQSPSQRVNLETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 459
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1953273547  460 AKDELGYCLTSIEAAIEYIR 479
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03095 PHA03095
ankyrin-like protein; Provisional
 872-1025 2.48e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 2.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  872 RADLIPLLLKHGANagarnVNQA-----VPLHLACQKGHFQ---VVRCLLDSKAKPNKKDISGNTPLI-YACSNGYHEVA 942
Cdd:PHA03095    26 TVEEVRRLLAAGAD-----VNFRgeygkTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVI 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  943 ALLLQHGASINICNNKGNTALHE--AVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCAEQNS----KIMELLQVVPSCV 1016
Cdd:PHA03095   101 KLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnanvELLRLLIDAGADV 180


                   ....*....
gi 1953273547 1017 ASVDDVGQT 1025
Cdd:PHA03095   181 YAVDDRFRS 189
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 841-990 3.27e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 3.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  841 KKLAKIPASGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQ-----VVRCLLDS 915
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEY 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  916 KAKPNKKDISGNTPLIYACSN--GYHEVAALLLQHGASINICNNKGNTALHEAVIEKHV--FVVELLLLHGASVQVVNK 990
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR 174
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-664 1.21e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:COG0666    182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                           90
                   ....*....|
gi 1953273547  655 YGHEDCVKAL 664
Cdd:COG0666    262 AGAALIVKLL 271
PHA03095 PHA03095
ankyrin-like protein; Provisional
 598-983 2.96e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 2.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  598 LVSRGAGVNATDYHGSAPLHLACQKGYQSVT---LLLLHYKASPEVQDNNGNTPLHL-ACAYGHEDCVKALVYYDVqscR 673
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGA---D 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  674 LDIGNEKGDTPLHIAAR--WGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKilsimeahhlplerrrkssevpvqpp 751
Cdd:PHA03095   110 VNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR-------------------------- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  752 qrpadsisqasstssfssvlassrqeepkkdyrevekllravaDGDLEMVRYLLewteedldeleDAAA-VGDVDFC--- 827
Cdd:PHA03095   164 -------------------------------------------NANVELLRLLI-----------DAGAdVYAVDDRfrs 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  828 --HPLCQCPRcaPAQKKLAKIPASGLGVNVTNQDGTSPLHVAALHG---RADLIPLLLKhGANAGARNVNQAVPLHLACQ 902
Cdd:PHA03095   190 llHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAV 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  903 KGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHE-VAALLLQHGASINICN--NKGNTALHEAVIEKHVFVVELLL 979
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSAETVAAtlNTASVAGGDIPSDATRLCVAKVV 346


                   ....
gi 1953273547  980 LHGA 983
Cdd:PHA03095   347 LRGA 350
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 546-582 3.63e-14

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: 67.28  E-value: 3.63e-14
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1953273547  546 MCHPLCFCDDCEKLVSGRLNDPSIVTPFSRDDRGHTP 582
Cdd:cd22883      2 FCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 575-723 3.66e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 3.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACA 654
Cdd:PHA02874   120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  655 YGHEDCVKALVyydVQSCRLDIGNEKGDTPLHIAARWGYQGIieTLLQNGASTEIQNRLKETPLNCALN 723
Cdd:PHA02874   200 YGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 848-999 6.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 6.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  848 ASGLGVNVTNQD-GTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISG 926
Cdd:PHA02878   155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953273547  927 NTPLIYACSNGY-HEVAALLLQHGASINICNN-KGNTALHEAVIEKHvfVVELLLLHGASVQVVNKRQCTAIDCA 999
Cdd:PHA02878   235 NTPLHISVGYCKdYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 850-1049 1.00e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 1.00e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTP 929
Cdd:PHA02874   147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  930 LIYACSngYHEVAALLLQHGASINICNNKGNTALHEAVIEK-HVFVVELLLLHGASVQVVNKRQCTAIDCAEQNSKIMEL 1008
Cdd:PHA02874   227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV 304

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1953273547 1009 LQVVPSCVASVDDVGQ---TDRKEYVTVKIRKKWNSKMYDLPDE 1049
Cdd:PHA02874   305 IKDIIANAVLIKEADKlkdSDFLEHIEIKDNKEFSDFIKECNEE 348
Ank_2 pfam12796
Ankyrin repeats (3 copies);
815-923 1.68e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  815 LEDAAAVGDVDFCHPLCQCprcapaqkklakipasGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHgaNAGARNVNQA 894
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN----------------GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGR 62

                           90       100
                   ....*....|....*....|....*....
gi 1953273547  895 VPLHLACQKGHFQVVRCLLDSKAKPNKKD 923
Cdd:pfam12796   63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 797-989 1.93e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  797 DLEMVRYLLEWTEEDLDELEDA-----AAVGDVDFCHPLCQcprcapaqkklakipaSGLGVNVTNQDGTSPLHVAALHG 871
Cdd:PLN03192   506 DLNVGDLLGDNGGEHDDPNMASnlltvASTGNAALLEELLK----------------AKLDPDIGDSKGRTPLHIAASKG 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  872 RADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKdiSGNTPLIYACSNGYHEVAALLLQHGAS 951
Cdd:PLN03192   570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLN 647

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1953273547  952 INICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVN 989
Cdd:PLN03192   648 VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 861-1009 2.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.46  E-value: 2.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  861 TSPLHVAALHGraDLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHE 940
Cdd:PHA02874    94 TSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  941 VAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA-EQNSKIMELL 1009
Cdd:PHA02874   172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiIHNRSAIELL 241
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 575-722 3.48e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 3.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKG-YQSVTLLLLHyKASPEVQDNNGNTPLHLAC 653
Cdd:PHA02874   153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGdYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  654 AYGhedcvKALVYYDVQSCRLDIGNEKGDTPLHIAARWG-YQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PHA02874   232 IHN-----RSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAF 296
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 577-722 5.27e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 5.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  577 DRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYg 656
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  657 hedcvkaLVYYDVQSCRLDIG---NEK----GDTPLHIAARwgYQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 591-724 2.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 2.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  591 QASLIDFLVSRGAGVNATDYH-GSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYdv 669
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  670 qSCRLDIGNEKGDTPLHIAArwGY---QGIIETLLQNGASTEIQNRLKE-TPLNCALNS 724
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISV--GYckdYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 849-1009 2.52e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.02  E-value: 2.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  849 SGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNK---KDis 925
Cdd:PHA02875    24 IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD-- 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  926 GNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTA--IDCAEQNS 1003
Cdd:PHA02875   102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPliIAMAKGDI 181


                   ....*.
gi 1953273547 1004 KIMELL 1009
Cdd:PHA02875   182 AICKML 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 596-986 3.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 3.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  596 DFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVyydvqSCRLD 675
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  676 IgnEKGDTPLHIAARwgyQGIIET---LLQNGASTEIQNRLKETPLNCALNSKILSimeahhlplerrrkssevpvqppq 752
Cdd:PHA02876   237 I--NKNDLSLLKAIR---NEDLETsllLYDAGFSVNSIDDCKNTPLHHASQAPSLS------------------------ 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  753 rpadsisqasstssfssvlassrqeepkkdyREVEKLLRAVADGDLEMVR-----YLLEWTEEDLDELEDAAAVG-DVD- 825
Cdd:PHA02876   288 -------------------------------RLVPKLLERGADVNAKNIKgetplYLMAKNGYDTENIRTLIMLGaDVNa 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  826 ----FCHPLCQCPRCAPAQKKLAKIPASGLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLA- 900
Cdd:PHA02876   337 adrlYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  901 CQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYH-EVAALLLQHGASINICNNKGNTALHEAvIEKHVfVVELLL 979
Cdd:PHA02876   417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILL 494


                   ....*..
gi 1953273547  980 LHGASVQ 986
Cdd:PHA02876   495 HYGAELR 501
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 873-1009 3.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  873 ADLIPLLLKHGANAGARNVNQ-AVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGAS 951
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  952 INICNNKGNTALHEAVIE-KHVFVVELLLLHGASVQVVNK-RQCTAIDCAEQNSKIMELL 1009
Cdd:PHA02878   227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLL 286
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 594-729 5.90e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 5.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  594 LIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTL--LLLHYKASPEVQDNNGNTPLHLACAYGHED--CVKALVY--Y 667
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDkgV 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  668 DVQS-----------CRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSI 729
Cdd:PHA03100   168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 683-1022 6.16e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 6.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  683 TPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEAhhlplerrrkssevpvqppqrpadsisqas 762
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA------------------------------ 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  763 stssfssvLASSRQEEPKKDYreveKLLRAVADGDLEMVRYLLEwteedldeleDAAAVGDVDFCH--PLCQCPRCAPAQ 840
Cdd:PHA02876   230 --------IIDNRSNINKNDL----SLLKAIRNEDLETSLLLYD----------AGFSVNSIDDCKntPLHHASQAPSLS 287

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  841 KKLAKIPASGLGVNVTNQDGTSPLHVAALHG-RADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQ-VVRCLLDSKAK 918
Cdd:PHA02876   288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGAN 367

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  919 PNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFV-VELLLLHGASVQVVNKRQCTAID 997
Cdd:PHA02876   368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLH 447

                          330       340
                   ....*....|....*....|....*
gi 1953273547  998 CAEQNSKIMELLQVVPSCVASVDDV 1022
Cdd:PHA02876   448 YACKKNCKLDVIEMLLDNGADVNAI 472
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 895-1009 6.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 6.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  895 VPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYH-----EVAALLLQHGASINICNNKGNTALHEAVIE 969
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1953273547  970 K--HVFVVELLLLHGASVQVVNKRQCTAI----DCAEQNSKIMELL 1009
Cdd:PHA03100   117 KsnSYSIVEYLLDNGANVNIKNSDGENLLhlylESNKIDLKILKLL 162
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 789-966 6.59e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 6.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  789 LLRAVADGDLEMVRYLLEWTEEdldeledaAAVGDVDFCHPLCQCPRcAPAQKKLAKIPASGLGVNVTNQDGTSPLHVAA 868
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIK-HNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  869 LHGRADLIPLLLKHGANAGARNVNQAVPLHLACQkgHFQVVRCLLDSKAKPNKKDISGNTPLIYA----CSNgyhEVAAL 944
Cdd:PHA02874   199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDI---DIIDI 273

                          170       180
                   ....*....|....*....|..
gi 1953273547  945 LLQHGASINICNNKGNTALHEA 966
Cdd:PHA02874   274 LLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 575-721 1.25e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAaLCGQ---ASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEV--QDNNGNTPL 649
Cdd:PHA03095   113 KDKVGRTPLHVY-LSGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGADVyaVDDRFRSLL 191

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273547  650 HLACAYGH--EDCVKALVyydVQSCRLDIGNEKGDTPLHIAARWG--YQGIIETLLQNGASTEIQNRLKETPLNCA 721
Cdd:PHA03095   192 HHHLQSFKprARIVRELI---RAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYA 264
PHA03095 PHA03095
ankyrin-like protein; Provisional
 797-964 1.35e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  797 DLEMVRYLLewteedldeledaAAVGDVDF-----CHPLCQCPRCApaQKKLAKIP----ASGLGVNVTNQDGTSPLHVA 867
Cdd:PHA03095    26 TVEEVRRLL-------------AAGADVNFrgeygKTPLHLYLHYS--SEKVKDIVrlllEAGADVNAPERCGFTPLHLY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  868 ALHG-RADLIPLLLKHGANAGARNVNQAVPLHlACQKG---HFQVVRCLLDSKAKPNKKDISGNTPL-IYACSNGYH-EV 941
Cdd:PHA03095    91 LYNAtTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRNANvEL 169

                          170       180
                   ....*....|....*....|...
gi 1953273547  942 AALLLQHGASINICNNKGNTALH 964
Cdd:PHA03095   170 LRLLIDAGADVYAVDDRFRSLLH 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 584-675 1.42e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.77  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  584 HVAAlCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKA 663
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|..
gi 1953273547  664 LVYYDVQSCRLD 675
Cdd:PTZ00322   167 LSRHSQCHFELG 178
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 510-722 2.27e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 2.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  510 TSTPidcLFKHIASGNQKEVERLLSQDDQDKDAVQRMCHPLcfcddcekLVSGRLNDPSIVTPFSRDDRGHTPLHVAalC 589
Cdd:PHA02874    35 TTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPL--------LTAIKIGAHDIIKLLIDNGVDTSILPIP--C 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  590 GQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYydv 669
Cdd:PHA02874   102 IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE--- 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  670 QSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PHA02874   179 KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 865-948 2.91e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.62  E-value: 2.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  865 HVAAlHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAAL 944
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1953273547  945 LLQH 948
Cdd:PTZ00322   167 LSRH 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
873-1009 4.58e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 4.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  873 ADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASI 952
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  953 NICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA--EQNSKIMELL 1009
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 780-988 6.31e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 6.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  780 KKDYREVEKLLRAVAD-------GDLEMVRYLLEWTEEDLDEL--EDAAAVGDVDFCH--PLCQCPRCAPAQKKLAKI-P 847
Cdd:PHA03095    60 EKVKDIVRLLLEAGADvnapercGFTPLHLYLYNATTLDVIKLliKAGADVNAKDKVGrtPLHVYLSGFNINPKVIRLlL 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  848 ASGLGVNVTNQDGTSPLHVAALHGRAD--LIPLLLKHGANAGARNVNQAVPLHLACQ--KGHFQVVRCLLDSKAKPNKKD 923
Cdd:PHA03095   140 RKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATD 219

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  924 ISGNTPLIYAC--SNGYHEVAALLLQHGASINICNNKGNTALHEAVI-EKHVFVVELLLLhGASVQVV 988
Cdd:PHA03095   220 MLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVfNNPRACRRLIAL-GADINAV 286
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 854-1005 1.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 1.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  854 NVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQA-VPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIY 932
Cdd:PHA02875    62 DVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  933 ACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDC-AEQNSKI 1005
Cdd:PHA02875   142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
Ank_2 pfam12796
Ankyrin repeats (3 copies);
572-642 2.32e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 2.32e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953273547  572 PFSRDDRGHTPLHVAALCGQASLIDFLVSRgAGVNATDYhGSAPLHLACQKGYQSVTLLLLHYKASPEVQD 642
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
896-946 4.83e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 4.83e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1953273547  896 PLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLL 946
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 826-863 5.32e-10

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: 55.34  E-value: 5.32e-10
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1953273547  826 FCHPLCQCPRCAPAQKKLAKIPaSGLGVNVTNQDGTSP 863
Cdd:cd22883      2 FCHPLCQCPKCAPAVSRLAKDP-SGVGVNSRDQDGRTP 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
926-979 1.30e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.30e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  926 GNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLL 979
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 850-1027 1.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISgntp 929
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  930 LIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVF-VVELLLLHGASVQVVNKRQCTAIDCAEQNSKIMEL 1008
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEN 323

                          170
                   ....*....|....*....
gi 1953273547 1009 LQVVPSCVAsvdDVGQTDR 1027
Cdd:PHA02876   324 IRTLIMLGA---DVNAADR 339
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 581-720 3.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  581 TPLHVAALCGQASLIDFLVSRGAGVNATDYH-GSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHED 659
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953273547  660 CVKALVyyDVQSCrLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNC 720
Cdd:PHA02875   150 GIELLI--DHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 583-731 4.16e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  583 LHVAALC-----GQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGh 657
Cdd:PHA02875     1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEG- 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  658 eDCVKALVYYDVQSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIME 731
Cdd:PHA02875    80 -DVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 556-729 4.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  556 CEKLVSGRLN------DPSIVTPFSRDDrGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKG-YQSVT 628
Cdd:PHA02875     7 CDAILFGELDiarrllDIGINPNFEIYD-GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  629 LLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYDVQScrlDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTE 708
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180
                   ....*....|....*....|.
gi 1953273547  709 IQNRLKETPLNCALNSKILSI 729
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAI 183
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 582-733 4.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 4.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  582 PLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQ---------------------------------------- 621
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  622 ------KGYQS------------------VTLLLLHYKASPEVQD-NNGNTPLHLACAYGHEDCVKALVYYDVQSCRLDI 676
Cdd:PHA02878   120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953273547  677 GNekgDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCA----LNSKILSIMEAH 733
Cdd:PHA02878   200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 565-702 4.55e-09

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: 60.48  E-value: 4.55e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  565 NDPSivtpFSRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNA------------TD--YHGSAPLHLACQKGYQSVTLL 630
Cdd:TIGR00870  118 NDQY----TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGESPLNAAACLGSPSIVAL 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  631 LLHYKASPEVQDNNGNTPLHLAC----------AYGHEdCVKALVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGI 696
Cdd:TIGR00870  194 LSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNHQGLTPLKLAAKEGRIVL 272


                   ....*.
gi 1953273547  697 IETLLQ 702
Cdd:TIGR00870  273 FRLKLA 278
PHA02798 PHA02798
ankyrin-like protein; Provisional
 874-998 4.93e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.23  E-value: 4.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  874 DLIPLLLKHGANAGARNVNQAVPL-----HLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGY---HEVAALL 945
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFM 131

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953273547  946 LQHGASINICNNKGNTALHEAVIEKH---VFVVELLLLHGASV-QVVNKRQCTAIDC 998
Cdd:PHA02798   132 IENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDInTHNNKEKYDTLHC 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
860-913 5.16e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 5.16e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  860 GTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLL 913
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 572-663 6.08e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 6.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  572 PFSRDDRGHTPLHVAALCG--QASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPL 649
Cdd:PHA03095   215 PAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                           90
                   ....*....|....
gi 1953273547  650 HLACAYGHEDCVKA 663
Cdd:PHA03095   295 SLMVRNNNGRAVRA 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 850-967 7.70e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 7.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQK-GHFQVVRCLLDSKAKPNKKD-ISGN 927
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyILGL 270

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1953273547  928 TPLIYACSNgyHEVAALLLQHGASINICNNKGNTALHEAV 967
Cdd:PHA02878   271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
612-665 8.75e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 8.75e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  612 GSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALV 665
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 578-710 1.33e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.12  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATD-------------YHGSAPLHL-ACQKGYQSVTLLLLH--YKASPEVQ 641
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLaACTNQEEIVRLLLENgaQPAALEAQ 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  642 DNNGNTPLH--------------LACAYGHEdcvkaLVYYDVQSCRL----DIGNEKGDTPLHIAARWGYQGIIETLLQN 703
Cdd:cd21882    152 DSLGNTVLHalvlqadntpensaFVCQMYNL-----LLSYGAHLDPTqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226


                   ....*..
gi 1953273547  704 GASTEIQ 710
Cdd:cd21882    227 EFSGPYQ 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 574-722 2.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  574 SRDDRGHTPLHVAALCGQAS-LIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTL-LLLHYKASPEVQDNNGNTPLHL 651
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953273547  652 ACAYG-HEDCVKALVYYDVQSCRLDIGNEkgdTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PHA02876   348 ASTLDrNKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 586-722 2.57e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  586 AALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALV 665
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953273547  666 YYdvqsCRLDIGNEKGDTpLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PLN03192   612 HF----ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAM 663
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 487-702 2.75e-08

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: 57.88  E-value: 2.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  487 PPESEGFGDRLFLKQRMSLLSQMT--STPIDCLFKHIAS--GNQKEVERLLSQDDQDKDAVQRMCHPLCfcddceklvsg 562
Cdd:cd22193      1 LEELLGFLQDLCRRRKDLTDSEFTesSTGKTCLMKALLNlnPGTNDTIRILLDIAEKTDNLKRFINAEY----------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  563 rlndpsivtpfsRDD--RGHTPLHVAALCGQASLIDFLVSRGAGVNATD--------------YHGSAPLHL-ACQKGYQ 625
Cdd:cd22193     70 ------------TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPD 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  626 SVTLLL--LHYKASPEVQDNNGNTPLHLACAYG-----HEDCVKALvyYD---VQSCRL-------DIGNEKGDTPLHIA 688
Cdd:cd22193    138 IVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLA 215

                          250
                   ....*....|....
gi 1953273547  689 ARWGYQGIIETLLQ 702
Cdd:cd22193    216 AKMGKIEILKYILQ 229
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 818-964 4.68e-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: 57.33  E-value: 4.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  818 AAAVGDVDFCHPLCQCPRCAPAQKklakipasglGVNvtnqdGTSPLHVAALHGRADLIPLLLkhgaNAGARNVNQAV-- 895
Cdd:cd22192     24 AAKENDVQAIKKLLKCPSCDLFQR----------GAL-----GETALHVAALYDNLEAAVVLM----EAAPELVNEPMts 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  896 -------PLHLACQKGHFQVVRCLLDSKA------------KPNKKDIS--GNTPLIYACSNGYHEVAALLLQHGASINI 954
Cdd:cd22192     85 dlyqgetALHIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 1953273547  955 CNNKGNTALH 964
Cdd:cd22192    165 QDSLGNTVLH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 578-665 8.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLACAYGH 657
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                   ....*...
gi 1953273547  658 EDCVKALV 665
Cdd:PHA02875   181 IAICKMLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 909-981 1.02e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.02e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  909 VRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLH 981
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
645-701 1.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953273547  645 GNTPLHLACAYGHEDCVKALVYYDVQSCRLDIGnekGDTPLHIAARWGYQGIIETLL 701
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 579-703 1.82e-07

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: 55.40  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  579 GHTPLHVAALCGQASLIDFLVSRGAGVN---ATD-----------YHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNN 644
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  645 GNTPLH---------LAC-AYgheDCVKALVYYDVQSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQN 703
Cdd:cd22192    169 GNTVLHilvlqpnktFACqMY---DLILSYDKEDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 581-722 1.83e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 1.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  581 TPLHvaalcgQASLID-------FLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLA- 652
Cdd:PHA02876   343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953273547  653 CAYGHEDCVKALVYydvQSCRLDIGNEKGDTPLHIAARWGYQ-GIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:PHA02876   417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
Ank_5 pfam13857
Ankyrin repeats (many copies);
630-688 2.48e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.48e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273547  630 LLLHYKASPEVQDNNGNTPLHLACAYGHEDCVKALVYYDVQscrLDIGNEKGDTPLHIA 688
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
605-652 5.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.87e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  605 VNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLHLA 652
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 577-661 5.98e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  577 DRGHTPLHVAALCGQaSLIDFLVSRgAGVNATDYHGSAPLHLA----CQKgyqSVTLLLLHYKASPEVQDNNGNTPLHLA 652
Cdd:PHA02874   221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                   ....*....
gi 1953273547  653 CAYGHEDCV 661
Cdd:PHA02874   296 FKYINKDPV 304
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 575-678 6.82e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 6.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVA-ALCGQASLIDFLVSRGAGVNATDY-HGSAPLHLACQKgyQSVTLLLLHYKASPEVQDNNGNTPLHLA 652
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                           90       100
                   ....*....|....*....|....*.
gi 1953273547  653 cayghedcvkALVYYDVQSCRLDIGN 678
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
Ank_5 pfam13857
Ankyrin repeats (many copies);
919-966 7.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.50e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  919 PNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEA 966
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
853-900 8.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 8.27e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  853 VNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHLA 900
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 926-957 1.39e-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: 1.39e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1953273547  926 GNTPLIYAC-SNGYHEVAALLLQHGASINICNN 957
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 575-718 1.76e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  575 RDDRGHTPLHVAALCGQAS--LIDFLVSRGAGVNATDYHGSAPLHLACQ--KGYQSVTLLLLHYKASPEVQDNNGNTPLH 650
Cdd:PHA03095   148 LDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLH 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  651 LACAYGhedcvkalvyydvqSCR-------------LDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETP 717
Cdd:PHA03095   228 SMATGS--------------SCKrslvlplliagisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293


                   .
gi 1953273547  718 L 718
Cdd:PHA03095   294 L 294
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 380-478 1.93e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 47.84  E-value: 1.93e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547   380 IPRAKRELAQLNKCTSPQQKLICLRKVVQLITQSPSQRVNlETMCADDLLSVLLYLLVKTDIPNWMANLSYIKNFRFSSS 459
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1953273547   460 AKDELGYCLTSIEAAIEYI 478
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 601-718 3.21e-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: 51.17  E-value: 3.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  601 RGAgvnatdyHGSAPLHLACQKGYQSVTLLLLhyKASPEVQDN-------NGNTPLHLACAYGHEDCVKALVYY--DVQS 671
Cdd:cd22192     47 RGA-------LGETALHVAALYDNLEAAVVLM--EAAPELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIARgaDVVS 117

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273547  672 CR-------LDIGN--EKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPL 718
Cdd:cd22192    118 PRatgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 926-954 3.45e-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: 44.50  E-value: 3.45e-06
                            10        20
                    ....*....|....*....|....*....
gi 1953273547   926 GNTPLIYACSNGYHEVAALLLQHGASINI 954
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
572-619 3.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.94e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  572 PFSRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLA 619
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 578-702 4.05e-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: 51.01  E-value: 4.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATD-------------YHGSAPLHL-ACQKGYQSVTLLL--LHYKASPEVQ 641
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953273547  642 DNNGNTPLHlACAYGHEDCVK--ALV--YYD---VQSCRLD-------IGNEKGDTPLHIAARWGYQGIIETLLQ 702
Cdd:cd22197    173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDgllQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
879-933 5.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273547  879 LLKHG-ANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYA 933
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 572-634 9.95e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 9.95e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  572 PFSRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHY 634
Cdd:PTZ00322   108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 644-669 2.08e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.08e-05
                            10        20
                    ....*....|....*....|....*.
gi 1953273547   644 NGNTPLHLACAYGHEDCVKALVYYDV 669
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 578-711 2.88e-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: 48.26  E-value: 2.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATD--------------YHGSAPLHL-ACQKGYQSVTLLLL--HYKASPEV 640
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  641 QDNNGNTPLH--LACAYGHEDCVKALV-YYD---VQSCRL-------DIGNEKGDTPLHIAARWGYQGIIETLLQNgast 707
Cdd:cd22196    173 RDSMGNTVLHalVEVADNTPENTKFVTkMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR---- 248


                   ....
gi 1953273547  708 EIQN 711
Cdd:cd22196    249 EIKE 252
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 576-711 3.23e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  576 DDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQdnNGNTPLHLACAY 655
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKR 632

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273547  656 GHEDCVKALVYydvQSCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQN 711
Cdd:PLN03192   633 NDLTAMKELLK---QGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 680-712 4.52e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 4.52e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1953273547  680 KGDTPLHIAA-RWGYQGIIETLLQNGASTEIQNR 712
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 958-990 6.56e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 6.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1953273547  958 KGNTALHEAVIE-KHVFVVELLLLHGASVQVVNK 990
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 892-1009 6.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  892 NQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKH 971
Cdd:PHA02875     1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1953273547  972 VFVVELLLLHGASVQ-VVNKRQCTAIDCAE--QNSKIMELL 1009
Cdd:PHA02875    81 VKAVEELLDLGKFADdVFYKDGMTPLHLATilKKLDIMKLL 121
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 578-701 1.43e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.90  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNATD--------------YHGSAPLHL-ACQKGYQSVTLLLLHYKASPEVQD 642
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  643 NNGNTPLHLACAYG-----HEDCVKALvyYD--VQSCR---LD-IGNEKGDTPLHIAARWGYQGIIETLL 701
Cdd:cd22194    220 SRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 926-954 1.85e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.85e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953273547  926 GNTPLIYACSNGYHEVAALLLQHGASINI 954
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 578-609 2.65e-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: 2.65e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1953273547  578 RGHTPLHVAAL-CGQASLIDFLVSRGAGVNATD 609
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 644-667 2.89e-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: 2.89e-04
                           10        20
                   ....*....|....*....|....*
gi 1953273547  644 NGNTPLHLACA-YGHEDCVKALVYY 667
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-732 3.55e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.48  E-value: 3.55e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  685 LHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSIMEA 732
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 867-1025 3.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  867 AALHGRADLIPLLLKHGANAGARNVNQAVPLHLACQKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLL 946
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  947 QHGASIN-ICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA--EQNSKIMELLQVVPSCVASVDDVG 1023
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAvmMGDIKGIELLIDHKACLDIEDCCG 168


                   ..
gi 1953273547 1024 QT 1025
Cdd:PHA02875   169 CT 170
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 546-582 3.89e-04

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: 38.84  E-value: 3.89e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1953273547  546 MCHPLCFCDDCEKLVSG-RLNDPSIVTPFSRDDRGHTP 582
Cdd:cd22886      5 LCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
959-999 4.66e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 4.66e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1953273547  959 GNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA 999
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
575-649 5.85e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 5.85e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953273547  575 RDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPL 649
Cdd:COG0666    215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 896-921 7.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.25e-04
                            10        20
                    ....*....|....*....|....*.
gi 1953273547   896 PLHLACQKGHFQVVRCLLDSKAKPNK 921
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 889-1024 8.40e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 8.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  889 RNVNQAVP-------LHLACQ-KG-HFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKG 959
Cdd:PHA02946    26 RNMLQAIEpsgnyhiLHAYCGiKGlDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQH 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273547  960 NTALH------EAVIEKhvfvVELLLLHGASV-QVVNKRQCTA-IDCAEQNSKIMELLQVVPSCVASVDDVGQ 1024
Cdd:PHA02946   106 KTPLYylsgtdDEVIER----INLLVQYGAKInNSVDEEGCGPlLACTDPSERVFKKIMSIGFEARIVDKFGK 174
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 569-702 9.48e-04

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: 43.30  E-value: 9.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  569 IVTPFsRD--DRGHTPLHVAALCGQASLIDFLVSRGAGVNATD--------------YHGSAPLHLA-CQKGYQSVTLLL 631
Cdd:cd22195    126 INSPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLT 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  632 --LHYKASPEVQDNNGNTPLH--LACAYGHEDCVKALV-YYDV---------QSCRLD-IGNEKGDTPLHIAARWGYQGI 696
Cdd:cd22195    205 enAHKKADLRRQDSRGNTVLHalVAIADNTRENTKFVTkMYDLllikcaklyPDCNLEaILNNDGMSPLMMAAKLGKIGI 284


                   ....*.
gi 1953273547  697 IETLLQ 702
Cdd:cd22195    285 FQHIIR 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 859-885 9.74e-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: 37.57  E-value: 9.74e-04
                            10        20
                    ....*....|....*....|....*..
gi 1953273547   859 DGTSPLHVAALHGRADLIPLLLKHGAN 885
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 644-669 1.19e-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: 1.19e-03
                           10        20
                   ....*....|....*....|....*.
gi 1953273547  644 NGNTPLHLACAYGHEDCVKALVYYDV 669
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA03095 PHA03095
ankyrin-like protein; Provisional
 568-665 1.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  568 SIVTPF--------SRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPE 639
Cdd:PHA03095   238 SLVLPLliagisinARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1953273547  640 VQDNNgntpLHLACAYGHED-------CVKALV 665
Cdd:PHA03095   318 TVAAT----LNTASVAGGDIpsdatrlCVAKVV 346
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 680-709 1.26e-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: 1.26e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953273547   680 KGDTPLHIAARWGYQGIIETLLQNGASTEI 709
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 896-923 1.35e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.35e-03
                           10        20
                   ....*....|....*....|....*....
gi 1953273547  896 PLHLAC-QKGHFQVVRCLLDSKAKPNKKD 923
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 902-979 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 1.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  902 QKGHFQVVRCLLDSKAKPNKKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLL 979
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 860-970 1.44e-03

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: 42.76  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  860 GTSPLHVAALHGRADLIPLLLKHGANAGAR-NVNqavplhlACQKGhfQVVRCLLDSKAKPNkkdisgntplIYACSnGY 938
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARaCGD-------FFVKS--QGVDSFYHGESPLN----------AAACL-GS 187

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1953273547  939 HEVAALLLQHGASINICNNKGNTALHEAVIEK 970
Cdd:TIGR00870  188 PSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 859-890 1.49e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.49e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1953273547  859 DGTSPLHVAALH-GRADLIPLLLKHGANAGARN 890
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
681-722 1.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.57e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1953273547  681 GDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCAL 722
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
579-632 1.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953273547  579 GHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLL 632
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 578-607 1.67e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.67e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1953273547   578 RGHTPLHVAALCGQASLIDFLVSRGAGVNA 607
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
945-999 1.76e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273547  945 LLQHG-ASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCA 999
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 958-985 2.00e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 2.00e-03
                            10        20
                    ....*....|....*....|....*...
gi 1953273547   958 KGNTALHEAVIEKHVFVVELLLLHGASV 985
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
671-718 2.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1953273547  671 SCRLDIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPL 718
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 578-607 2.14e-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: 2.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953273547  578 RGHTPLHVAALCGQASLIDFLVSRGAGVNA 607
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 942-1026 2.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  942 AALLLQHGASINICNNKGNTALHEAVIEKHVFVVELLLLHGASVQVVNKRQCTAIDCAEQNS--KIMELLQVVPSCVASV 1019
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQLLSRHSQCHFEL 177


                   ....*..
gi 1953273547 1020 DDVGQTD 1026
Cdd:PTZ00322   178 GANAKPD 184
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 905-999 2.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 2.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  905 HFQVVRCLLDSKAKPN----KKDISGNTPLIYACSNGYHEVAALLLQHGASINICNNKGN-TALHEAVIEKHVFVVELLL 979
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILL 124

                           90       100
                   ....*....|....*....|
gi 1953273547  980 LHGASVQVVNKRQCTAIDCA 999
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 555-676 3.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  555 DCEKLVSGRLNDPSIvtpfSRDDRgHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHY 634
Cdd:PHA02875   116 DIMKLLIARGADPDI----PNTDK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1953273547  635 KASPEVQDNNGntplhlacayghedCVKALVyYDVQSCRLDI 676
Cdd:PHA02875   191 GANIDYFGKNG--------------CVAALC-YAIENNKIDI 217
PHA02946 PHA02946
ankyin-like protein; Provisional
 850-968 3.51e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  850 GLGVNVTNQDGTSPLHVAALHGRADLIPLLLKHGANAGARNVNQAVPLHL--ACQKGHFQVVRCLLDSKAKPNKK-DISG 926
Cdd:PHA02946    62 GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSvDEEG 141

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1953273547  927 NTPLIyACSNGYHEVAALLLQHGASINICNNKGNTALHEAVI 968
Cdd:PHA02946   142 CGPLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLM 182
PHA02946 PHA02946
ankyin-like protein; Provisional
 571-718 3.66e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  571 TPFSRDDRGHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLAC---QKGYQSVTLLLLHYKASPEVQDNNGNT 647
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  648 PLhLACAYGHEDCVKALVYYDVQS----------------------------CRLDIGNEK----GDTPLHIAARWGYQG 695
Cdd:PHA02946   144 PL-LACTDPSERVFKKIMSIGFEArivdkfgknhihrhlmsdnpkastiswmMKLGISPSKpdhdGNTPLHIVCSKTVKN 222

                          170       180
                   ....*....|....*....|....
gi 1953273547  696 I-IETLLQNGASTEIQNRLKETPL 718
Cdd:PHA02946   223 VdIINLLLPSTDVNKQNKFGDSPL 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 675-729 4.24e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 4.24e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1953273547  675 DIGNEKGDTPLHIAARWGYQGIIETLLQNGASTEIQNRLKETPLNCALNSKILSI 729
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI 606
PHA02946 PHA02946
ankyin-like protein; Provisional
 547-651 4.54e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273547  547 CHPLCFCDDCEKLVSGRLN----DPSIVTPFSRDdrgHTPLHVAALCGQASLIDFLVSRGAGVNATDYHGSAPLHLACQK 622
Cdd:PHA02946   142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                           90       100       110
                   ....*....|....*....|....*....|
gi 1953273547  623 GYQSVTLL-LLHYKASPEVQDNNGNTPLHL 651
Cdd:PHA02946   219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTL 248
PHA02946 PHA02946
ankyin-like protein; Provisional
 587-650 5.12e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 5.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273547  587 ALCGQASL----IDFLVSRGAGVNATDYHGSAPLHLACQKGYQSVTLLLLHYKASPEVQDNNGNTPLH 650
Cdd:PHA02946    43 AYCGIKGLderfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
 
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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