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Conserved domains on  [gi|1958647249|ref|XP_017444845|]
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ankyrin repeat domain-containing protein 27 isoform X1 [Rattus norvegicus]

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];
725-894 3.80e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPN 804
Cdd:COG0666     68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCAE 884
Cdd:COG0666    148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227

                          170
                   ....*....|..
gi 1958647249  885 Q--DSKIMELLQ 894
Cdd:COG0666    228 EngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.06e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.79e-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: 82.30  E-value: 1.79e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958647249  429 KMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 super family cl19569
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.49e-15

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.


The actual alignment was detected with superfamily member pfam02204:

Pssm-ID: 473191  Cd Length: 104  Bit Score: 71.86  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1958647249  344 PKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
Ank_2 super family cl48147
Ankyrin repeats (3 copies);
387-493 1.49e-04

Ankyrin repeats (3 copies);


The actual alignment was detected with superfamily member pfam12796:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  387 MNLLSQMSSTPidcLFKHIASGNQKEVERLLSQDDQDkdamqkmchplcscedceklvsgrlndpsvvtpfsRDDRGQTP 466
Cdd:pfam12796   23 ANLQDKNGRTA---LHLAAKNGHLEIVKLLLEHADVN-----------------------------------LKDNGRTA 64

                           90       100
                   ....*....|....*....|....*..
gi 1958647249  467 LHVAALCGQASLIDFLVSKGAVVNATD 493
Cdd:pfam12796   65 LHYAARSGHLEIVKLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-894 3.80e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPN 804
Cdd:COG0666     68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCAE 884
Cdd:COG0666    148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227

                          170
                   ....*....|..
gi 1958647249  885 Q--DSKIMELLQ 894
Cdd:COG0666    228 EngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.06e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-873 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  781 LHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHgAAINACNNkGNTALHEAVMGRHVLVVE 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958647249  861 LLLFYGASVDILN 873
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 2.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  500 LHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1958647249  580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 1.69e-19

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: 82.37  E-value: 1.69e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958647249  706 VDLEFCHPLCQCPKCAPAQKKLARIPANGLSVNVTNQDGFSP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.79e-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: 82.30  E-value: 1.79e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958647249  429 KMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 703-874 1.85e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  703 ISTVDLEFCHPLCQCpkcapAQKKLARIP------ANGLSVNVTNQDGFSPLHMAALHGRTDL--VPLLLKHGAYSGARN 774
Cdd:PHA03100    99 VNAPDNNGITPLLYA-----ISKKSNSYSiveyllDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKN 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  775 tsqavplhlacqqghfqVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGR 854
Cdd:PHA03100   174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                          170       180
                   ....*....|....*....|
gi 1958647249  855 HVLVVELLLFYGASVDILNK 874
Cdd:PHA03100   237 NKEIFKLLLNNGPSIKTIIE 256
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.49e-15

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: 71.86  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1958647249  344 PKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-589 2.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 2.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  520 ANTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 371-586 8.75e-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: 56.34  E-value: 8.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  371 PPDAEGFGDRLfLKQRMNLLSQM---SSTPIDCLFKHIAS--GNQKEVERLLSQDDQDKDAMqkmchplcscedceklvs 445
Cdd:cd22193      1 LEELLGFLQDL-CRRRKDLTDSEfteSSTGKTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  446 grlnDPSVVTPFsRDD--RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGF 508
Cdd:cd22193     62 ----KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQP 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  509 QSVTLLL--LHYKANTEVQDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHI 571
Cdd:cd22193    137 DIVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQL 214

                          250
                   ....*....|....*
gi 1958647249  572 AARWGYEGIIETLLQ 586
Cdd:cd22193    215 AAKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 2.86e-07

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: 54.70  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  437 CEDC----EKLVSGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  498 TPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 1958647249  564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-838 3.23e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.23e-05
                            10        20
                    ....*....|....*....|....*....
gi 1958647249   810 GNTPLICACSAGHHEVAALLLQHGAAINA 838
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 4.63e-05

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 43.98  E-value: 4.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1958647249   344 PKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
Ank_2 pfam12796
Ankyrin repeats (3 copies);
387-493 1.49e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  387 MNLLSQMSSTPidcLFKHIASGNQKEVERLLSQDDQDkdamqkmchplcscedceklvsgrlndpsvvtpfsRDDRGQTP 466
Cdd:pfam12796   23 ANLQDKNGRTA---LHLAAKNGHLEIVKLLLEHADVN-----------------------------------LKDNGRTA 64

                           90       100
                   ....*....|....*....|....*..
gi 1958647249  467 LHVAALCGQASLIDFLVSKGAVVNATD 493
Cdd:pfam12796   65 LHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.17e-04
                            10        20
                    ....*....|....*....|....*.
gi 1958647249   528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-894 3.80e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPN 804
Cdd:COG0666     68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCAE 884
Cdd:COG0666    148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227

                          170
                   ....*....|..
gi 1958647249  885 Q--DSKIMELLQ 894
Cdd:COG0666    228 EngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
673-883 2.82e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 2.82e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  673 LLRAVADGDLEMVRYLLEwteddlddmdeaistvdlefchplcqcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAA 752
Cdd:COG0666     91 LHAAARNGDLEIVKLLLE------------------------------------------AGADVNARDKDGETPLHLAA 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  753 LHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQH 832
Cdd:COG0666    129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  833 GAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA 883
Cdd:COG0666    209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-879 4.36e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 4.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  476 ASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVqa 555
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  556 cRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLkcalnskilsameayhlssdrrpkpsevpapsp 635
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  636 trsadsisqgsstssfssvsvsfrpeevkkdyreveklLRAVADGDLEMVRYLLEwteddlddmdeaistvdlefchplc 715
Cdd:COG0666    125 --------------------------------------HLAAYNGNLEIVKLLLE------------------------- 141

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  716 qcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKC 795
Cdd:COG0666    142 -----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  796 LLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKR 875
Cdd:COG0666    205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284


                   ....
gi 1958647249  876 QYTA 879
Cdd:COG0666    285 LLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 1.06e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 1.06e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-893 2.22e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPN 804
Cdd:COG0666     35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA- 883
Cdd:COG0666    115 ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAa 194

                          170
                   ....*....|.
gi 1958647249  884 -EQDSKIMELL 893
Cdd:COG0666    195 eNGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
460-847 2.80e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 2.80e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  460 DDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTY 539
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  540 GQEDCVKALVYYDVQacrLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLkcalnskilsameayhl 619
Cdd:COG0666     98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL----------------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  620 ssdrrpkpsevpapsptrsadsisqgsstssfssvsvsfrpeevkkdyreveklLRAVADGDLEMVRYLLEwteddlddm 699
Cdd:COG0666    158 ------------------------------------------------------HLAAANGNLEIVKLLLE--------- 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  700 deaistvdlefchplcqcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAV 779
Cdd:COG0666    175 ---------------------------------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT 221

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  780 PLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTAL 847
Cdd:COG0666    222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-611 8.38e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 8.38e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACT 538
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647249  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKIL 611
Cdd:COG0666    196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
457-814 1.17e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  457 FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLA 536
Cdd:COG0666     48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  537 CTYGQEDCVKALVYY--DVqacrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLkcalnskilsam 614
Cdd:COG0666    128 AYNGNLEIVKLLLEAgaDV-----NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL------------ 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  615 eayHLssdrrpkpsevpapsptrsadsisqgsstssfssvsvsfrpeevkkdyrevekllrAVADGDLEMVRYLLEwted 694
Cdd:COG0666    191 ---HL--------------------------------------------------------AAENGHLEIVKLLLE---- 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  695 dlddmdeaistvdlefchplcqcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARN 774
Cdd:COG0666    208 --------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1958647249  775 TSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPL 814
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
725-893 3.26e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 3.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPN 804
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA- 883
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAa 161

                          170
                   ....*....|.
gi 1958647249  884 -EQDSKIMELL 893
Cdd:COG0666    162 aNGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
781-873 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.99e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  781 LHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHgAAINACNNkGNTALHEAVMGRHVLVVE 860
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958647249  861 LLLFYGASVDILN 873
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 2.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.71e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  500 LHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1958647249  580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
748-838 1.42e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.42e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  748 LHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDsNAKPNKRDlSGNTPLICACSAGHHEVAA 827
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1958647249  828 LLLQHGAAINA 838
Cdd:pfam12796   79 LLLEKGADINV 89
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 706-747 1.69e-19

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: 82.37  E-value: 1.69e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958647249  706 VDLEFCHPLCQCPKCAPAQKKLARIPANGLSVNVTNQDGFSP 747
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKRTARLPKSGLNVNSCNSDGFTP 42
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.79e-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: 82.30  E-value: 1.79e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958647249  429 KMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-559 5.89e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.89e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  467 LHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKANTevqDNNGNTPLHLACTYGQEDCV 545
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGhLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958647249  546 KALVYYDVQACRLD 559
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 703-874 1.85e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  703 ISTVDLEFCHPLCQCpkcapAQKKLARIP------ANGLSVNVTNQDGFSPLHMAALHGRTDL--VPLLLKHGAYSGARN 774
Cdd:PHA03100    99 VNAPDNNGITPLLYA-----ISKKSNSYSiveyllDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKN 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  775 tsqavplhlacqqghfqVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGR 854
Cdd:PHA03100   174 -----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                          170       180
                   ....*....|....*....|
gi 1958647249  855 HVLVVELLLFYGASVDILNK 874
Cdd:PHA03100   237 NKEIFKLLLNNGPSIKTIIE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 738-872 1.04e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 1.04e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  738 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICA 817
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647249  818 CSAGHHEVAALLLQHGAAINACNNKGN-TALHEAVMGRHVLVVELLLFYGASVDIL 872
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.49e-15

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: 71.86  E-value: 4.49e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1958647249  344 PKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 696-883 6.79e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.77  E-value: 6.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  696 LDDMDEAISTVDLEFchpLCQCPKCAPAQKKLARIP-ANGLSVNVTNQD-GFSPLHMAALHGRTDLVPLLLKHGAYSGAR 773
Cdd:PHA02878   121 LTNRYKNIQTIDLVY---IDKKSKDDIIEAEITKLLlSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIP 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  774 NTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPL-ICACSAGHHEVAALLLQHGAAINACNN-KGNTALHEAV 851
Cdd:PHA02878   198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI 277

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1958647249  852 MGRHVLvvELLLFYGASVDILNKRQYTAVDCA 883
Cdd:PHA02878   278 KSERKL--KLLLEYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 482-870 1.02e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 1.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  482 LVSKGAVVNATDYHGSTPLHLACQKGFQSVT---LLLLHYKANTEVQDNNGNTPLHLACTYGQ-EDCVKALVYY--DVQA 555
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  556 CrldigNEKGDTALHIAAR--WGYEGIIETLLQNGA-PTAIQNRLKeTPLKCALNSKilsameayhlssdrrpkpsevpa 632
Cdd:PHA03095   113 K-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGAdVNALDLYGM-TPLAVLLKSR----------------------- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  633 psptrsadsisqgsstssfssvsvsfrpeevkkdyrevekllravaDGDLEMVRYLLEWTEDdlddmdeaISTVDLEF-- 710
Cdd:PHA03095   164 ----------------------------------------------NANVELLRLLIDAGAD--------VYAVDDRFrs 189

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  711 -CHPLCQCPKcaPAQKKLARIPANGLSVNVTNQDGFSPLHMAALHG---RTDLVPLLLKhGAYSGARNTSQAVPLHLACQ 786
Cdd:PHA03095   190 lLHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAV 266

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  787 QGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHE-VAALLLQH------GAAINACNNKGNTALHEAvmgRHVLVV 859
Cdd:PHA03095   267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNpsaetvAATLNTASVAGGDIPSDA---TRLCVA 343

                          410
                   ....*....|.
gi 1958647249  860 ELLLFYGASVD 870
Cdd:PHA03095   344 KVVLRGAFSLL 354
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-589 2.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 2.23e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  520 ANTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 3.39e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.46  E-value: 3.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  461 DRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYg 540
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647249  541 qedcvkaLVYYDVQACRLDIG---NEK----GDTALHIAARwgYEGIIETLLQNGAPTAIQNRLKETPLKCAL 606
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
673-807 1.20e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  673 LLRAVADGDLEMVRYLLEwteddlddmdeaistvdlefchplcqcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAA 752
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE------------------------------------------NGADANLQDKNGRTALHLAA 38

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  753 LHGRTDLVPLLLKHGAysGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRD 807
Cdd:pfam12796   39 KNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 478-611 1.33e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 1.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  478 LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHYKANTEVQDNNGNTPLHLA--CTYGQEDCVKALVY--Y 551
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDkgV 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  552 DVQA-----------CRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKIL 611
Cdd:PHA03100   168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 387-607 1.56e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  387 MNLLSQMSSTPidcLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSC-----EDCEKLVSGRLNDPSV-------- 453
Cdd:PHA02874    28 INISVDETTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigaHDIIKLLIDNGVDTSIlpipciek 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  454 ----------VTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTE 523
Cdd:PHA02874   105 dmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  524 VQDNNGNTPLHLACTYGQEDCVKALVyydVQACRLDIGNEKGDTALHIAARWGYEGIieTLLQNGAPTAIQNRLKETPLK 603
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLH 259


                   ....
gi 1958647249  604 CALN 607
Cdd:PHA02874   260 HAIN 263
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 1.57e-13

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: 65.35  E-value: 1.57e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1958647249  429 KMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 727-878 1.84e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.49  E-value: 1.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  727 LARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNkr 806
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD-- 95

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  807 DL---SGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYT 878
Cdd:PHA02875    96 DVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 480-869 1.03e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  480 DFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVyydvqACRLD 559
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  560 IgnEKGDTALHIAARwgYEGIIETLLQNGAPTAIQ--NRLKETPLKCALNSKILSAMEayhlssdrrPKPSEvpapsptR 637
Cdd:PHA02876   237 I--NKNDLSLLKAIR--NEDLETSLLLYDAGFSVNsiDDCKNTPLHHASQAPSLSRLV---------PKLLE-------R 296

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  638 SADSisqgsstssfssvsvsfrpeEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDdlddmdeaISTVDLEFCHPLCQC 717
Cdd:PHA02876   297 GADV--------------------NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQA 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  718 PKCAPAQKKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA-CQQGHFQVAKCL 796
Cdd:PHA02876   349 STLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTL 428

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  797 LDSNAKPNKRDLSGNTPLICACSAG-HHEVAALLLQHGAAINACNNKGNTALHEAvMGRHVlVVELLLFYGASV 869
Cdd:PHA02876   429 IDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 734-893 3.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  734 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTP 813
Cdd:PHA02874   147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  814 LICACSagHHEVAALLLQHGAAINACNNKGNTALHEAVMGR-HVLVVELLLFYGASVDILNKRQYTAVDCA----EQDSK 888
Cdd:PHA02874   227 LHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAfkyiNKDPV 304


                   ....*
gi 1958647249  889 IMELL 893
Cdd:PHA02874   305 IKDII 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 727-874 7.07e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 7.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  727 LARIPANGLSVNVTNQDGFSPLHM---AALHGRTDLVPLLLKHGAYSGARNTSQAVPLHL-ACQQGHFQVAKCLLDSNAK 802
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGAD 109

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  803 PNKRDLSGNTPL-ICACS-AGHHEVAALLLQHGAAINACNNKGNTALHeAVMGRHVLVVELL-LFYGASVDILNK 874
Cdd:PHA03095   110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELLrLLIDAGADVYAV 183
PHA03095 PHA03095
ankyrin-like protein; Provisional
 758-882 7.45e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 7.45e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  758 DLVPLLLKHGA---YSGARNTSqavPLHLACQQGHFQVAK---CLLDSNAKPNKRDLSGNTPLIC-ACSAGHHEVAALLL 830
Cdd:PHA03095    28 EEVRRLLAAGAdvnFRGEYGKT---PLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  831 QHGAAINACNNKGNTALHE--AVMGRHVLVVELLLFYGASVDILNKRQYTAVDC 882
Cdd:PHA03095   105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 734-863 8.72e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 8.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  734 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTP 813
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  814 LICACSAGHHEVAALLLQHGAAI-NACNNkGNTALHEAVMGRHVlVVELLL 863
Cdd:PHA02874   194 LHNAAEYGDYACIKLLIDHGNHImNKCKN-GFTPLHNAIIHNRS-AIELLI 242
Ank_4 pfam13637
Ankyrin repeats (many copies);
810-863 1.69e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.69e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  810 GNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLL 863
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 733-880 1.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 1.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  733 NGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNKRDl 808
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN- 173

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  809 sgntplicacsaghheVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAV 880
Cdd:PHA03100   174 ----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 2.19e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.19e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKgAVVNATDYhGSTPLHLACQKGFQSVTLLLLHYKANTEVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 460-551 2.26e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 68.00  E-value: 2.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  460 DDRGQTPLHVAA--LC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTP 532
Cdd:PTZ00322    72 EVIDPVVAHMLTveLCqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                           90
                   ....*....|....*....
gi 1958647249  533 LHLACTYGQEDCVKALVYY 551
Cdd:PTZ00322   152 LELAEENGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 725-893 2.50e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  725 KKLARIPANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHfqvakclldsNAKPN 804
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY----------NLTDV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KrdlsgntplicacsaghhEVAALLLQHGAAINACNNKGNTALHEAVMGR--HVLVVELLLFYGASVDILNKRQYT---- 878
Cdd:PHA03100    86 K------------------EIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENllhl 147

                          170
                   ....*....|....*
gi 1958647249  879 AVDCAEQDSKIMELL 893
Cdd:PHA03100   148 YLESNKIDLKILKLL 162
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-608 4.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 4.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  475 QASLIDFLVSKGAVVNATDYH-GSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYdv 553
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  554 qACRLDIGNEKGDTALHIAARW--GYEgIIETLLQNGAPTAIQNRLKE-TPLKCALNS 608
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISVGYckDYD-ILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 757-893 3.22e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 3.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  757 TDLVPLLLKHGAYSGARNTSQ-AVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAA 835
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  836 INACNNKGNTALHEAVmGR--HVLVVELLLFYGASVDILNK-RQYTAVDCAEQDSKIMELL 893
Cdd:PHA02878   227 TDARDKCGNTPLHISV-GYckDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLL 286
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-896 6.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 6.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  567 TALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAMEAYhlsSDRRPKPSevpapsptrsadsisqgs 646
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI---IDNRSNIN------------------ 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  647 stssfssvsvsfrpeevKKDYreveKLLRAVADGDLEmvryllewTEDDLDDMDEAISTVDLEFCHPLCQCPKCAPAQKK 726
Cdd:PHA02876   239 -----------------KNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  727 LARIPANGLSVNVTNQDGFSPLHMAALHG-RTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-VAKCLLDSNAKPN 804
Cdd:PHA02876   290 VPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVN 369

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  805 KRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRH-VLVVELLLFYGASVDILNKRQYTAVDCA 883
Cdd:PHA02876   370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                          330
                   ....*....|...
gi 1958647249  884 EQDSKIMELLQVV 896
Cdd:PHA02876   450 CKKNCKLDVIEML 462
PHA02798 PHA02798
ankyrin-like protein; Provisional
 757-882 6.61e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 62.93  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  757 TDLVPLLLKHGAYSGARNTSQAVPL-----HLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGH---HEVAAL 828
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  829 LLQHGAAINACNNKGNTALHEAVMGRHVL---VVELLLFYGASVDIL-NKRQYTAVDC 882
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHnNKEKYDTLHC 188
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 709-747 1.58e-09

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: 54.18  E-value: 1.58e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958647249  709 EFCHPLCQCPKCAPAQKKLARIPAnGLSVNVTNQDGFSP 747
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPS-GVGVNSRDQDGRTP 38
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 738-832 2.85e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 2.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  738 NVTNQDGFSP--LHMAALH-------GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDL 808
Cdd:PTZ00322    67 NLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                           90       100
                   ....*....|....*....|....
gi 1958647249  809 SGNTPLICACSAGHHEVAALLLQH 832
Cdd:PTZ00322   147 DGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 734-854 2.94e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  734 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQ-GHFQVAKCLLDSNAKPN-KRDLSGN 811
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGL 270

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958647249  812 TPLicACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGR 854
Cdd:PHA02878   271 TAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
780-830 2.98e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.98e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  780 PLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLL 830
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 670-883 6.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 6.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  670 VEKLLRAVADGDLEMVRYLLEWTEDdlddmdeaISTVDLEFCHPLCQCPKCApAQKKLARIPANGLSVNVtnqdgfspLH 749
Cdd:PHA02874    36 TTPLIDAIRSGDAKIVELFIKHGAD--------INHINTKIPHPLLTAIKIG-AHDIIKLLIDNGVDTSI--------LP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  750 MAALHgrTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALL 829
Cdd:PHA02874    99 IPCIE--KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  830 LQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA 883
Cdd:PHA02874   177 LEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 732-837 6.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 6.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  732 ANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSGN 811
Cdd:PHA02875   123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                           90       100
                   ....*....|....*....|....*..
gi 1958647249  812 TPLIC-ACSAGHHEVAALLLQHGAAIN 837
Cdd:PHA02875   203 VAALCyAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 3.96e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  461 DRGQTPLHVAALCGQaSLIDFLVSKgAVVNATDYHGSTPLHLA----CQKgfqSVTLLLLHYKANTEVQDNNGNTPLHLA 536
Cdd:PHA02874   221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                   ....*....
gi 1958647249  537 CTYGQEDCV 545
Cdd:PHA02874   296 FKYINKDPV 304
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-589 5.72e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  470 AALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPL---------------- 533
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  534 HLA------------CTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:PLN03192   612 HFAsisdphaagdllCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 7.19e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 7.19e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958647249  529 GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGnekGDTALHIAARWGYEGIIETLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-593 7.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 7.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958647249  542 EDCVKALVyyDVQAcRLDIGNEKGD-TALHIAARWGYEGIIETLLQNGAPTAI 593
Cdd:PHA02875   181 IAICKMLL--DSGA-NIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 793-928 7.73e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  793 AKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDIL 872
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  873 NKR----QYTAVDCAEQDSKIMEL---LQVVPSCVAASPNNVVVVQETEHEDYVTVEIRK--KWN 928
Cdd:PTZ00322   178 GANakpdSFTGKPPSLEDSPISSHhpdFSAVPQPMMGSLIVIMVGLPGRGKTYVARQIQRyfQWN 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 463-609 8.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  463 GQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  542 EDCVKALVYYDVQAcrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSK 609
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 371-586 8.75e-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: 56.34  E-value: 8.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  371 PPDAEGFGDRLfLKQRMNLLSQM---SSTPIDCLFKHIAS--GNQKEVERLLSQDDQDKDAMqkmchplcscedceklvs 445
Cdd:cd22193      1 LEELLGFLQDL-CRRRKDLTDSEfteSSTGKTCLMKALLNlnPGTNDTIRILLDIAEKTDNL------------------ 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  446 grlnDPSVVTPFsRDD--RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGF 508
Cdd:cd22193     62 ----KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQP 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  509 QSVTLLL--LHYKANTEVQDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHI 571
Cdd:cd22193    137 DIVQYLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQL 214

                          250
                   ....*....|....*
gi 1958647249  572 AARWGYEGIIETLLQ 586
Cdd:cd22193    215 AAKMGKIEILKYILQ 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 396-547 1.02e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 1.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  396 TPIDCLFKhiaSGN-QKEVERLL---SQDDQDKDA-MQKMCHPLC-SCEDCEKLVsgRLNDPSVVTPFSRDDRGQTPLHV 469
Cdd:PHA03095   154 TPLAVLLK---SRNaNVELLRLLidaGADVYAVDDrFRSLLHHHLqSFKPRARIV--RELIRAGCDPAATDMLGNTPLHS 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  470 AALCG--QASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKA 547
Cdd:PHA03095   229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 416-518 1.10e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  416 LLSQDDQDKDAMQKMCHPLCSCEDCEKLVSGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYH 495
Cdd:PTZ00322    68 LTTEEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                           90       100
                   ....*....|....*....|...
gi 1958647249  496 GSTPLHLACQKGFQSVTLLLLHY 518
Cdd:PTZ00322   148 GKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 724-873 1.36e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  724 QKKLARIPANGLSVNVTNQDG----FSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDS 799
Cdd:PLN03192   501 HKELHDLNVGDLLGDNGGEHDdpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  800 NAKPNKRDLSGNTPLICACSAGHHEV-------AAL------------------------LLQHGAAINACNNKGNTALH 848
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHHKIfrilyhfASIsdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQ 660

                          170       180
                   ....*....|....*....|....*
gi 1958647249  849 EAVMGRHVLVVELLLFYGASVDILN 873
Cdd:PLN03192   661 VAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
746-797 1.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  746 SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL 797
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 2.86e-07

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: 54.70  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  437 CEDC----EKLVSGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  498 TPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 1958647249  564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 734-878 3.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 3.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  734 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKRDLSgntp 813
Cdd:PHA02876   168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS---- 243

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647249  814 LICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHV-LVVELLLFYGASVDILNKRQYT 878
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGET 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-549 4.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  496 GSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALV 549
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-589 5.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 5.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  458 SRDDRGQTPLHVAALCGQAS-LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL-LLLHYKANTEVQDNNGNTPLHL 535
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  536 ACTYGQ-EDCVKALVYYDVQACRLDIGNEkgdTALHIAARWGYEGIIETLLQNGA 589
Cdd:PHA02876   348 ASTLDRnKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGA 399
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 5.70e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647249  482 LVSKGAV-VNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 462-585 8.72e-07

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: 53.22  E-value: 8.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLLHYKANTEVQD 526
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  527 NNGNTPLHLACTYG-----QEDCVKALvyYD--VQACR---LD-IGNEKGDTALHIAARWGYEGIIETLL 585
Cdd:cd22194    220 SRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 1.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  459 RDDRGQTPLHVA-ALCGQASLIDFLVSKGAVVNATDY-HGSTPLHLACQKgfQSVTLLLLHYKANTEVQDNNGNTPLHLA 536
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                           90       100
                   ....*....|....*....|....*.
gi 1958647249  537 ctygqedcvkALVYYDVQACRLDIGN 562
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 465-606 1.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  465 TPLHvaalcgQASLID-------FLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLA- 536
Cdd:PHA02876   343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  537 CTYGQEDCVKALVYydvQACRLDIGNEKGDTALHIAARWGYE-GIIETLLQNGAPTAIQNRLKETPLKCAL 606
Cdd:PHA02876   417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 1.58e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 1.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  463 GQTPLHVAALCGQASLIDFLVSKGAVVN---ATD-----------YHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNN 528
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  529 GNTPLHLACTygQEDCVKALVYYDV---------QACRLDIGNEKGDTALHIAARWGYEGIIETLLQN 587
Cdd:cd22192    169 GNTVLHILVL--QPNKTFACQMYDLilsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 1.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.58e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958647249  456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 2.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.88e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647249  514 LLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQacrLDIGNEKGDTALHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-841 3.02e-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: 44.59  E-value: 3.02e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958647249  810 GNTPLICAC-SAGHHEVAALLLQHGAAINACNN 841
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-516 4.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  465 TPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLL 516
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-850 7.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 7.60e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1958647249  803 PNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEA 850
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 1.15e-05

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 43.08  E-value: 1.15e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958647249  428 QKMCHPLCSCEDCEKLVSG-RLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22886      3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
735-784 1.34e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.34e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958647249  735 LSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA 784
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 462-586 1.53e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.03  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLL--HYKANTEV 524
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  525 QDNNGNTPLHLACTYG---QEDCVKALVYYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22196    173 RDSMGNTVLHALVEVAdntPENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 467-615 1.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  467 LHVAALC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875     1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  542 EDCVKALVyyDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSKILSAME 615
Cdd:PHA02875    81 VKAVEELL--DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 744-852 2.37e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 2.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  744 GFSPLHMAALHGRTDLVPLLLKHGA-YSGARNTSQAVPLHlacqqghfqvAKCLLdsnakpnkrdLSGNTPLICACSAGH 822
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGAdVVSPRATGTFFRPG----------PKNLI----------YYGEHPLSFAACVGN 148

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958647249  823 HEVAALLLQHGAAINACNNKGNTALHEAVM 852
Cdd:cd22192    149 EEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 810-838 3.23e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 3.23e-05
                            10        20
                    ....*....|....*....|....*....
gi 1958647249   810 GNTPLICACSAGHHEVAALLLQHGAAINA 838
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 458-528 3.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 3.26e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958647249  458 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKANTEVQDNN 528
Cdd:PHA03100   187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 842-874 4.31e-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: 4.31e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958647249  842 KGNTALHEAV-MGRHVLVVELLLFYGASVDILNK 874
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 796-912 4.35e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 4.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  796 LLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDilnkr 875
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD----- 618

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958647249  876 QYTAVDcaeqdskimeLLqvvpsCVAASPNNVVVVQE 912
Cdd:PLN03192   619 PHAAGD----------LL-----CTAAKRNDLTAMKE 640
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 4.63e-05

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 43.98  E-value: 4.63e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETVCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1958647249   344 PKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-589 8.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 8.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  458 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA-CQKGFQSVTLLLLHYKANTEVQDNNGNTPLHLA 536
Cdd:PHA02876   370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958647249  537 CTYG-QEDCVKALVYYDVQACRLDIGNEkgdTALHIAArwGYEGIIETLLQNGA 589
Cdd:PHA02876   450 CKKNcKLDVIEMLLDNGADVNAINIQNQ---YPLLIAL--EYHGIVNILLHYGA 498
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 1.27e-04

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: 46.00  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD-------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKANTEVQ 525
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958647249  526 DNNGNTPLHlACTYGQEDCVK--ALV--YYD--VQA-CRLD-------IGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22197    173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDglLQAgARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
387-493 1.49e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  387 MNLLSQMSSTPidcLFKHIASGNQKEVERLLSQDDQDkdamqkmchplcscedceklvsgrlndpsvvtpfsRDDRGQTP 466
Cdd:pfam12796   23 ANLQDKNGRTA---LHLAAKNGHLEIVKLLLEHADVN-----------------------------------LKDNGRTA 64

                           90       100
                   ....*....|....*....|....*..
gi 1958647249  467 LHVAALCGQASLIDFLVSKGAVVNATD 493
Cdd:pfam12796   65 LHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.17e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.17e-04
                            10        20
                    ....*....|....*....|....*.
gi 1958647249   528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-559 2.30e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  455 TPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHY--KANTEVqDNNGN 530
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERinLLVQYgaKINNSV-DEEGC 142

                           90       100
                   ....*....|....*....|....*....
gi 1958647249  531 TPLhLACTYGQEDCVKALVYYDVQACRLD 559
Cdd:PHA02946   143 GPL-LACTDPSERVFKKIMSIGFEARIVD 170
PHA02946 PHA02946
ankyin-like protein; Provisional
 796-870 2.64e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.64e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958647249  796 LLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHeAVMGRHVLVVE---LLLFYGASVD 870
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKIN 134
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 810-838 2.95e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.95e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958647249  810 GNTPLICACSAGHHEVAALLLQHGAAINA 838
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 3.04e-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: 3.04e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958647249  462 RGQTPLHVAAL-CGQASLIDFLVSKGAVVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
829-883 3.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.65e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647249  829 LLQHG-AAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA 883
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
673-764 3.95e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  673 LLRAVADGDLEMVRYLLEwteddlddmdeaistvdlefchplcqcpkcapaqkklaripaNGLSVNVTNQDGFSPLHMAA 752
Cdd:pfam13637    5 LHAAAASGHLELLRLLLE------------------------------------------KGADINAVDGNGETALHFAA 42

                           90
                   ....*....|..
gi 1958647249  753 LHGRTDLVPLLL 764
Cdd:pfam13637   43 SNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 4.78e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.78e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958647249  564 KGDTALHIAA-RWGYEGIIETLLQNGAPTAIQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 743-768 4.85e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.85e-04
                            10        20
                    ....*....|....*....|....*.
gi 1958647249   743 DGFSPLHMAALHGRTDLVPLLLKHGA 768
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-602 5.95e-04

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: 43.85  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  416 LLSQDDQDKDAMQKmchpLCSCEDCEklvsgrlndpsvvtPFSRDDRGQTPLHVAALCGQASLIDFLVSKG-AVVN--AT 492
Cdd:cd22192     22 LLAAKENDVQAIKK----LLKCPSCD--------------LFQRGALGETALHVAALYDNLEAAVVLMEAApELVNepMT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  493 D--YHGSTPLHLACQKgfQSVTL--LLLHYKANTevqdnngNTPlhLACTYGQEDCVKALVYYdvqacrldignekGDTA 568
Cdd:cd22192     84 SdlYQGETALHIAVVN--QNLNLvrELIARGADV-------VSP--RATGTFFRPGPKNLIYY-------------GEHP 139

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958647249  569 LHIAARWGYEGIIETLLQNGAPTAIQNRLKETPL 602
Cdd:cd22192    140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-768 8.02e-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: 37.62  E-value: 8.02e-04
                           10        20
                   ....*....|....*....|....*.
gi 1958647249  743 DGFSPLHMAALHGRTDLVPLLLKHGA 768
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 9.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 9.96e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958647249  565 GDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 788-893 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  788 GHFQVAKCLLDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGA 867
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100
                   ....*....|....*....|....*....
gi 1958647249  868 SV-DILNKRQYTAVDCAE--QDSKIMELL 893
Cdd:PHA02875    93 FAdDVFYKDGMTPLHLATilKKLDIMKLL 121
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-602 1.15e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  514 LLLHYKANTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDignEKGDTALHIAARWGYEGIIETLLQ------- 586
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRhsqchfe 176

                           90       100
                   ....*....|....*....|..
gi 1958647249  587 ---NGAP---TAIQNRLKETPL 602
Cdd:PTZ00322   177 lgaNAKPdsfTGKPPSLEDSPI 198
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 711-749 1.22e-03

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


Pssm-ID: 439265 [Multi-domain]  Cd Length: 40  Bit Score: 37.62  E-value: 1.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958647249  711 CHPLCQCPKCapaQKKLARIPANGLSVNVTNQD--GFSPLH 749
Cdd:cd22885      3 CHPLCSCDKC---EKLLSGNRNDPSAVTVYSRDdrGYTALH 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 1.43e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.43e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958647249   462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-589 1.44e-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: 1.44e-03
                            10        20
                    ....*....|....*....|....*.
gi 1958647249   564 KGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 842-871 1.49e-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: 1.49e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958647249   842 KGNTALHEAVMGRHVLVVELLLFYGASVDI 871
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 690-828 1.74e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  690 EWTEDDLDDMDEAIS---TVDLefchplcqCPKCAPAQKKLARIP-ANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLK 765
Cdd:PTZ00322    65 DHNLTTEEVIDPVVAhmlTVEL--------CQLAASGDAVGARILlTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE 136

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  766 HGAYSGARNTSQAVPLHLACQQGHFQVAKCLL---------DSNAKPNKRDLSGNTPLICACSAGHHEVAAL 828
Cdd:PTZ00322   137 FGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKPDSFTGKPPSLEDSPISSHHPDFSAV 208
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 743-774 1.88e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.88e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958647249  743 DGFSPLHMAALH-GRTDLVPLLLKHGAYSGARN 774
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 780-805 2.14e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.14e-03
                            10        20
                    ....*....|....*....|....*.
gi 1958647249   780 PLHLACQQGHFQVAKCLLDSNAKPNK 805
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 842-871 2.25e-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: 2.25e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958647249  842 KGNTALHEAVMGRHVLVVELLLFYGASVDI 871
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 431-535 2.39e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  431 CHPLCSCEDCEKLVSGRLN----DPSVVTPFSRDdrgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQK 506
Cdd:PHA02946   142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958647249  507 GFQSVTLL-LLHYKANTEVQDNNGNTPLHL 535
Cdd:PHA02946   219 TVKNVDIInLLLPSTDVNKQNKFGDSPLTL 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-491 2.97e-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: 36.08  E-value: 2.97e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958647249  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 3.13e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|....*
gi 1958647249  528 NGNTPLHLACT-YGQEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 457-571 3.51e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  457 FSRDDRGQTPLHVAAL---CGQASLIDFLV-------SKGAVVNA--TD--YHGSTPLHLACQK-GFQSVTLLL-----L 516
Cdd:cd21882     20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLeaapdsgNPKELVNApcTDefYQGQTALHIAIENrNLNLVRLLVengadV 99

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647249  517 HYKANTEVQDNNGNT-------PLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHI 571
Cdd:cd21882    100 SARATGRFFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHA 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
843-883 3.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 3.96e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958647249  843 GNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCA 883
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 455-534 4.04e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 40.99  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  455 TPFsRD--DRGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHLA-CQKGFQSVTLLL-- 515
Cdd:cd22195    128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                           90
                   ....*....|....*....
gi 1958647249  516 LHYKANTEVQDNNGNTPLH 534
Cdd:cd22195    207 AHKKADLRRQDSRGNTVLH 225
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 797-883 4.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 4.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  797 LDSNAKPNKRDLSGNTPLICACSAGHHEVAALLLQHGAAINACNNKGN-TALHEAVMGRHVLVVELLLFYGASVDILNKR 875
Cdd:PHA02884    57 ADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTND 136


                   ....*...
gi 1958647249  876 QYTAVDCA 883
Cdd:PHA02884   137 MVTPIELA 144
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 825-920 4.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  825 VAALLLQHGAAINACNNKGNTALHEAVMGRHVLVVELLLFYGASVDILNKRQYTAVDCAEQDSKIMELLQVVPSCVAASP 904
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90
                   ....*....|....*.
gi 1958647249  905 NNVVVVQETEHEDYVT 920
Cdd:PHA02876   240 NDLSLLKAIRNEDLET 255
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 780-869 5.43e-03

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: 40.77  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  780 PLHLACQQGHFQVAKCLLDSN-AKPNKRDLSGNTPLICACSAGHHEVAALLLQhgAAINACNN-------KGNTALHEAV 851
Cdd:cd22192     20 PLLLAAKENDVQAIKKLLKCPsCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIAV 97

                           90
                   ....*....|....*...
gi 1958647249  852 MGRHVLVVELLLFYGASV 869
Cdd:cd22192     98 VNQNLNLVRELIARGADV 115
PHA02741 PHA02741
hypothetical protein; Provisional
 454-536 5.52e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 5.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647249  454 VTPFSR-----------DDRGQTPLHVAALCGQA----SLIDFLVSKGAVVNATD-YHGSTPLHLAC-QKGFQSVTLLLL 516
Cdd:PHA02741    40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAhRRDHDLAEWLCC 119

                           90       100
                   ....*....|....*....|
gi 1958647249  517 HYKANTEVQDNNGNTPLHLA 536
Cdd:PHA02741   120 QPGIDLHFCNADNKSPFELA 139
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-553 6.39e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.39e-03
                           10        20
                   ....*....|....*....|....*.
gi 1958647249  528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-625 7.90e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.24  E-value: 7.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647249  559 DIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAIQNRLKETPLKCALNSK------ILsameaYHLSSDRRP 625
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkifrIL-----YHFASISDP 619
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 495-527 8.21e-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: 34.96  E-value: 8.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958647249  495 HGSTPLHLAC-QKGFQSVTLLLLHYKANTEVQDN 527
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
 
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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