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Conserved domains on  [gi|1720422697|ref|XP_030098450|]
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ankyrin repeat domain-containing protein 27 isoform X2 [Mus musculus]

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];
519-689 3.10e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 519 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 598
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 599 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 678
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 1720422697 679 EQ--DSKIMELLQ 689
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
255-412 1.84e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 255 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 334
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 335 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 412
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 225-264 1.30e-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: 1.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720422697 225 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 264
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). ...
 60-159 2.29e-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: 72.63  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697  60 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 139
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1720422697 140 AKDELGYCLTSVEAAIEYIR 159
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
519-689 3.10e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 519 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 598
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 599 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 678
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 1720422697 679 EQ--DSKIMELLQ 689
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
255-412 1.84e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 255 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 334
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 335 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 412
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
576-668 6.12e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 6.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 576 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 655
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720422697 656 LLLFYGASVDILN 668
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
296-385 8.92e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 8.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 296 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 375
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 1720422697 376 IIETLLQNGA 385
Cdd:pfam12796  76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 225-264 1.30e-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: 1.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720422697 225 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 264
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 525-669 6.31e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 525 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 600
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 601 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 664
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1720422697 665 DILNK 669
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 502-542 1.61e-17

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.59  E-value: 1.61e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720422697 502 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 542
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 60-159 2.29e-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: 72.63  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697  60 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 139
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1720422697 140 AKDELGYCLTSVEAAIEYIR 159
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 256-418 1.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 256 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 315
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 316 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 392
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720422697 393 ---LKETPLKCALNSKIL--SIMEAHHLSSD 418
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 171-382 4.69e-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: 56.73  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 171 EGFGDRLfLKQRMNLL-SQMT--STPIDCLFKHIAS--GNQKEVERLLSQDDQDKDAMqkmchplcscedceklisgrln 245
Cdd:cd22193     5 LGFLQDL-CRRRKDLTdSEFTesSTGKTCLMKALLNlnPGTNDTIRILLDIAEKTDNL---------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 246 DPSVVTPFsRDD--RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVT 308
Cdd:cd22193    62 KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 309 LLL--LHYKASTEVQDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARW 371
Cdd:cd22193   141 YLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKM 218

                         250
                  ....*....|.
gi 1720422697 372 GYEGIIETLLQ 382
Cdd:cd22193   219 GKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 233-382 2.93e-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: 54.32  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 233 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 293
Cdd:TIGR00870  97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 294 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 359
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                         170       180
                  ....*....|....*....|...
gi 1720422697 360 KGDTALHIAARWGYEGIIETLLQ 382
Cdd:TIGR00870 256 QGLTPLKLAAKEGRIVLFRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 60-158 3.75e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.68  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697   60 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 139
Cdd:smart00167   2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90
                   ....*....|....*....
gi 1720422697  140 AKDELGYCLTSVEAAIEYI 158
Cdd:smart00167  81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 605-633 6.71e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 6.71e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720422697  605 GNTPLICACSAGHHEVAALLLQHGASINA 633
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 324-349 2.08e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.08e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720422697  324 NGNTPLHLACTYGQEDCVKALVYYDV 349
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
519-689 3.10e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 3.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 519 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 598
Cdd:COG0666    67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 599 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 678
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                         170
                  ....*....|...
gi 1720422697 679 EQ--DSKIMELLQ 689
Cdd:COG0666   227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
469-678 3.56e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 3.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 469 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 548
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE-----------------------------------------AGADVNARDKDGETPLHLAAY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 549 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHG 628
Cdd:COG0666   130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720422697 629 ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 678
Cdd:COG0666   210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
272-675 9.50e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 9.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 272 ASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVqa 351
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 352 cRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsimeahhlssdrrprpsevpaqsp 431
Cdd:COG0666    79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL--------------------------------- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 432 trsvdsisqgsstssfssisvsfrqeevkkdyreveklLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplc 511
Cdd:COG0666   125 --------------------------------------HLAAYNGNLEIVKLLLE------------------------- 141

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 512 qcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCL 591
Cdd:COG0666   142 ----------------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 592 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQ 671
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                  ....
gi 1720422697 672 YTAA 675
Cdd:COG0666   286 LTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
521-688 8.06e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.39  E-value: 8.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 521 KLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNK 600
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 601 KDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA-- 678
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAae 195

                         170
                  ....*....|
gi 1720422697 679 EQDSKIMELL 688
Cdd:COG0666   196 NGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
255-412 1.84e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 255 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 334
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 335 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 412
Cdd:COG0666   163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
256-642 1.29e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 256 DDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTY 335
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 336 GQEDCVKALVYYDVQacrLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPlkcalnskilsimeahhl 415
Cdd:COG0666    98 GDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP------------------ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 416 ssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekLLRAVADGDLEMVRYLLEwteddlddv 495
Cdd:COG0666   157 -----------------------------------------------------LHLAAANGNLEIVKLLLE--------- 174

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 496 edaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVP 575
Cdd:COG0666   175 --------------------------------AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720422697 576 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTAL 642
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
255-412 2.05e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 255 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 334
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 335 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 412
Cdd:COG0666   196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-609 4.23e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 253 FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 332
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 333 CTYGQEDCVKALVYY--DVqacrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLkcalnskilsim 410
Cdd:COG0666   128 AYNGNLEIVKLLLEAgaDV-----NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL------------ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 411 eahHLssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllrAVADGDLEMVRYLLEwted 490
Cdd:COG0666   191 ---HL--------------------------------------------------------AAENGHLEIVKLLLE---- 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 491 dlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNT 570
Cdd:COG0666   208 -------------------------------------AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1720422697 571 SQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPL 609
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
519-688 6.19e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 6.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 519 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 598
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 599 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA---A 675
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlA 160

                         170
                  ....*....|...
gi 1720422697 676 dCAEQDSKIMELL 688
Cdd:COG0666   161 -AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
576-668 6.12e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 6.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 576 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 655
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720422697 656 LLLFYGASVDILN 668
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
543-633 2.42e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 543 LHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDsNAKPNKKDlSGNTPLICACSAGHHEVAA 622
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1720422697 623 LLLQHGASINA 633
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
296-385 8.92e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 8.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 296 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 375
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 1720422697 376 IIETLLQNGA 385
Cdd:pfam12796  76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 225-264 1.30e-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: 1.30e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720422697 225 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 264
Cdd:cd22885     1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 525-669 6.31e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 6.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 525 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 600
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 601 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 664
Cdd:PHA03100  172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1720422697 665 DILNK 669
Cdd:PHA03100  252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 502-542 1.61e-17

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


Pssm-ID: 439266 [Multi-domain]  Cd Length: 42  Bit Score: 76.59  E-value: 1.61e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720422697 502 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 542
Cdd:cd22886     1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
263-355 1.63e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 263 LHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEvqDNNGNTPLHLACTYGQEDCVK 342
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720422697 343 ALVYYDVQACRLD 355
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 533-667 5.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 5.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 533 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICA 612
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422697 613 CSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDIL 667
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 60-159 2.29e-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: 72.63  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697  60 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 139
Cdd:pfam02204   1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                          90       100
                  ....*....|....*....|
gi 1720422697 140 AKDELGYCLTSVEAAIEYIR 159
Cdd:pfam02204  81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 527-668 7.39e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 7.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 527 ANGLSVNVTNQD-GFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSG 605
Cdd:PHA02878  155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 606 NTPL-ICACSAGHHEVAALLLQHGASINACNN-KGNTALHEAVmgRHTLVVELLLFYGASVDILN 668
Cdd:PHA02878  235 NTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLN 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 256-418 1.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 256 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 315
Cdd:PHA03100  103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 316 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 392
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720422697 393 ---LKETPLKCALNSKIL--SIMEAHHLSSD 418
Cdd:PHA03100  258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 183-403 1.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 183 MNLLSQMTSTPidcLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSC-----EDCEKLISGRLNDPSV-------- 249
Cdd:PHA02874   28 INISVDETTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigaHDIIKLLIDNGVDTSIlpipciek 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 250 ----------VTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTE 319
Cdd:PHA02874  105 dmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 320 VQDNNGNTPLHLACTYGQEDCVKALVyydVQACRLDIGNEKGDTALHIAARWGYEGIieTLLQNGAPTAVQNRLKETPLK 399
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLH 259


                  ....
gi 1720422697 400 CALN 403
Cdd:PHA02874  260 HAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 257-402 8.22e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 8.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 257 DRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYg 336
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422697 337 qedcvkaLVYYDVQACRLDIG---NEK----GDTALHIAARwgYEGIIETLLQNGAPTAVQNRLKETPLKCAL 402
Cdd:PHA02878  245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-602 8.41e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 469 LLRAVADGDLEMVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklarisaNGLSVNVTNQDGFSPLHMAAL 548
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-----------------------------------------NGADANLQDKNGRTALHLAAK 39

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 549 HGRTDLVPLLLKHGAysGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKD 602
Cdd:pfam12796  40 NGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 524-672 1.77e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 524 RISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-----VAKCLLDSNAKP 598
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 599 NKKDLSGNTPLICACSA--GHHEVAALLLQHGASINACNNKGNTALHEAVMGRH--TLVVELLLFYGASVDILNKRQY 672
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 529-683 2.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 2.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 529 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTP 608
Cdd:PHA02874  114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 609 LICACSAGHHEVAALLLQHGASI-NACNNkGNTALHEAVMGRHTlVVELL--------------------LFYGASVDIL 667
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGNHImNKCKN-GFTPLHNAIIHNRS-AIELLinnasindqdidgstplhhaINPPCDIDII 271

                         170
                  ....*....|....*.
gi 1720422697 668 NKRQYTAADCAEQDSK 683
Cdd:PHA02874  272 DILLYHKADISIKDNK 287
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 225-262 3.09e-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: 64.20  E-value: 3.09e-13
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720422697 225 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTP 262
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 278-665 3.19e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 278 LVSKGAVVNATDYHGSTPLHLACQKGFQSVT---LLLLHYKASTEVQDNNGNTPLHLACTYGQ-EDCVKALVYY--DVQA 351
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVNA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 352 CrldigNEKGDTALHIAAR--WGYEGIIETLLQNGA-PTAVQNRLKeTPLKCALNSKilsimeahhlssdrrprpsevpa 428
Cdd:PHA03095  113 K-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGAdVNALDLYGM-TPLAVLLKSR----------------------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 429 qsptrsvdsisqgsstssfssisvsfrqeevkkdyrevekllravaDGDLEMVRYLLEWTEDdlddvedaISTVDLEF-- 506
Cdd:PHA03095  164 ----------------------------------------------NANVELLRLLIDAGAD--------VYAVDDRFrs 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 507 -CHPLCQCPKcAPAQKLARISANGLSVNVTNQDGFSPLHMAALHG---RTDLVPLLLKhGAYSGARNTSQAVPLHLACQQ 582
Cdd:PHA03095  190 lLHHHLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVF 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 583 GHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHE-VAALLLQH------GASINACNNKGNTALHEAvmgRHTLVVE 655
Cdd:PHA03095  268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNpsaetvAATLNTASVAGGDIPSDA---TRLCVAK 344

                         410
                  ....*....|
gi 1720422697 656 LLLFYGASVD 665
Cdd:PHA03095  345 VVLRGAFSLL 354
PHA03095 PHA03095
ankyrin-like protein; Provisional
 522-669 3.42e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 3.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 522 LARISANGLSVNVTNQDGFSPLHM---AALHGRTDLVPLLLKHGAYSGARNTSQAVPLHL-ACQQGHFQVAKCLLDSNAK 597
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGAD 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 598 PNKKDLSGNTPL-ICACS-AGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVELL-LFYGASVDILNK 669
Cdd:PHA03095  110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELLrLLIDAGADVYAV 183
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 274-409 3.94e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 274 LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHYKASTEVQDNNGNTPLHLA--CTYGQEDCVKALVY--Y 347
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDkgV 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422697 348 DVQA-----------CRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 409
Cdd:PHA03100  168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 276-664 7.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 7.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 276 DFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVyydvqACRLD 355
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 356 IgnEKGDTALHIAARwgYEGIIETLLQNGAPTAVQ--NRLKETPLkcalnskilsimeaHHLSsdRRPRPSEVPAQSPTR 433
Cdd:PHA02876  237 I--NKNDLSLLKAIR--NEDLETSLLLYDAGFSVNsiDDCKNTPL--------------HHAS--QAPSLSRLVPKLLER 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 434 SVDSisqgsstssfssisvsfrqeEVKKDYREVEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQc 513
Cdd:PHA02876  297 GADV--------------------NAKNIKGETPLYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQ- 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 514 pkcapAQKLAR-----ISANGLSVNVTNQDGF--SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA-CQQGHF 585
Cdd:PHA02876  348 -----ASTLDRnkdivITLLELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 586 QVAKCLLDSNAKPNKKDLSGNTPLICACSAG-HHEVAALLLQHGASINACNNKGNTALHEAvMGRHTlVVELLLFYGASV 664
Cdd:PHA02876  423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 553-677 1.03e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 553 DLVPLLLKHGA---YSGARNTSqavPLHLACQQGHFQVAK---CLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 625
Cdd:PHA03095   28 EEVRRLLAAGAdvnFRGEYGKT---PLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 626 QHGASINACNNKGNTALHE--AVMGRHTLVVELLLFYGASVDILNKRQYTAADC 677
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 469-657 7.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.45  E-value: 7.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 469 LLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 548
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGAD--------VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 549 HGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQqgHFQVAKCLLDSNAKPNKKDLSGNTPLICA----CSAghhEVAALL 624
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDI---DIIDIL 274

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720422697 625 LQHGASINACNNKGNTALHEAV--MGRHTLVVELL 657
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
605-658 1.26e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.26e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 605 GNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLL 658
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 574-688 2.81e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 574 VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHH-----EVAALLLQHGASINACNNKGNTALHEAVMG 648
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720422697 649 R--HTLVVELLLFYGASVDILNKRQYT----AADCAEQDSKIMELL 688
Cdd:PHA03100  117 KsnSYSIVEYLLDNGANVNIKNSDGENllhlYLESNKIDLKILKLL 162
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 256-347 3.40e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 66.85  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 256 DDRGQTPLHVAA--LC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTP 328
Cdd:PTZ00322   72 EVIDPVVAHMLTveLCqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                          90
                  ....*....|....*....
gi 1720422697 329 LHLACTYGQEDCVKALVYY 347
Cdd:PTZ00322  152 LELAEENGFREVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
252-322 5.44e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 5.44e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 252 PFSRDDRGQTPLHVAALCGQASLIDFLVSKgAVVNATDYhGSTPLHLACQKGFQSVTLLLLHYKASTEVQD 322
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 552-703 2.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 552 TDLVPLLLKHGAYSGARNTSQ-AVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGAS 630
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422697 631 INACNNKGNTALHEAVmGR--HTLVVELLLFYGASVDILNK-RQYTAADCAEQDSKIMELLQVVPGCVASLDSVEE 703
Cdd:PHA02878  227 TDARDKCGNTPLHISV-GYckDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKL 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 271-404 2.92e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 271 QASLIDFLVSKGAVVNATDYH-GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdv 349
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 350 qACRLDIGNEKGDTALHIAARW--GYEgIIETLLQNGAPTAVQNRLKE-TPLKCALNS 404
Cdd:PHA02878  224 -GASTDARDKCGNTPLHISVGYckDYD-ILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02798 PHA02798
ankyrin-like protein; Provisional
 552-677 3.79e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.32  E-value: 3.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 552 TDLVPLLLKHGAYSGARNTSQAVPL-----HLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGH---HEVAAL 623
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 624 LLQHGASINACNNKGNTALHEAVMGRHTL---VVELLLFYGASVDIL-NKRQYTAADC 677
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHnNKEKYDTLHC 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 518-649 4.56e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 4.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 518 PAQKLAR-ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQ-GHFQVAKCLLDSN 595
Cdd:PHA02878  179 KDQRLTElLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 596 AKPNKKD-LSGNTPLicACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGR 649
Cdd:PHA02878  259 VDVNAKSyILGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 466-673 1.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 466 VEKLLRAVADGDLEMVRYLLEWTEDdlddvedaISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVtnqdgfspLHM 545
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGAD--------INHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 546 AALHgrTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 625
Cdd:PHA02874  100 PCIE--KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422697 626 QHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYT 673
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 529-674 2.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 529 GLSVNVTNQDGFSPLHMAA-LHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH-FQVAKCLLDSNAKPNKKDLSGN 606
Cdd:PHA02876  263 GFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720422697 607 TPLICACSAGHH-EVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA 674
Cdd:PHA02876  343 TPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 469-684 2.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 469 LLRAVADGDLEMVRYLLEWTEDDLDDVEDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAAL 548
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGIS--------PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 549 HGRTDLVPLLLKHGAYSGARNTSQA-VPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQH 627
Cdd:PHA02875   78 EGDVKAVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDH 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 628 GASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADC-AEQDSKI 684
Cdd:PHA02875  158 KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKI 215
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 469-632 2.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 469 LLRAVADGDLEMVRYLLEwTEDDLDDV--EDAIStvdlefchPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMA 546
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLD-LGKFADDVfyKDGMT--------PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 547 ALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 625
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFI 222


                  ....*..
gi 1720422697 626 QHGASIN 632
Cdd:PHA02875  223 KRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 533-627 2.85e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 533 NVTNQDGFSP--LHMAALH-------GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDL 603
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                          90       100
                  ....*....|....*....|....
gi 1720422697 604 SGNTPLICACSAGHHEVAALLLQH 627
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 529-668 4.41e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 4.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 529 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKdlSGNTP 608
Cdd:PLN03192  548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDL 625

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 609 LICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILN 668
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
575-625 5.48e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 5.48e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 575 PLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 625
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 363-669 1.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 363 TALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEAhhlssdrrprpsevpaqsptrSVDSisqgs 442
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKA---------------------IIDN----- 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 443 stssfssisvsfRQEEVKKDYreveKLLRAVADGDLEmvryllewTEDDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKL 522
Cdd:PHA02876  234 ------------RSNINKNDL----SLLKAIRNEDLE--------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRL 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 523 A-RISANGLSVNVTNQDGFSPLHMAALHG-RTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-VAKCLLDSNAKPN 599
Cdd:PHA02876  290 VpKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVN 369

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 600 KKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLV-VELLLFYGASVDILNK 669
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNK 440
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 505-542 2.34e-08

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: 50.72  E-value: 2.34e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720422697 505 EFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSP 542
Cdd:cd22883     1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 262-413 3.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 3.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 262 PLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQ---------------------------------------- 301
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnklgmkemirsinkcsvfytlvaikdafnnrnveifki 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 302 ------KGFQS------------------VTLLLLHYKASTEVQD-NNGNTPLHLACTYGQEDCVKALVYYDVQACRLDI 356
Cdd:PHA02878  120 iltnryKNIQTidlvyidkkskddiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 357 GNekgDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCA----LNSKILSIMEAH 413
Cdd:PHA02878  200 TN---NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgycKDYDILKLLLEH 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 527-666 3.46e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 527 ANGLSVNVTNQDGFSPLHmaALHGRTD----LVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 600
Cdd:PHA03095  140 RKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAA 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 601 KDLSGNTPL-----ICACSAGHheVAALLLqHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDI 666
Cdd:PHA03095  218 TDMLGNTPLhsmatGSSCKRSL--VLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 171-382 4.69e-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: 56.73  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 171 EGFGDRLfLKQRMNLL-SQMT--STPIDCLFKHIAS--GNQKEVERLLSQDDQDKDAMqkmchplcscedceklisgrln 245
Cdd:cd22193     5 LGFLQDL-CRRRKDLTdSEFTesSTGKTCLMKALLNlnPGTNDTIRILLDIAEKTDNL---------------------- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 246 DPSVVTPFsRDD--RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVT 308
Cdd:cd22193    62 KRFINAEY-TDEyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 309 LLL--LHYKASTEVQDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARW 371
Cdd:cd22193   141 YLLenEHQPADIEAQDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKM 218

                         250
                  ....*....|.
gi 1720422697 372 GYEGIIETLLQ 382
Cdd:cd22193   219 GKIEILKYILQ 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 257-341 4.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 257 DRGQTPLHVAALCGQaSLIDFLVSKgAVVNATDYHGSTPLHLA----CQKgfqSVTLLLLHYKASTEVQDNNGNTPLHLA 332
Cdd:PHA02874  221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                  ....*....
gi 1720422697 333 CTYGQEDCV 341
Cdd:PHA02874  296 FKYINKDPV 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 259-409 4.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 259 GQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 337
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720422697 338 EDCVKALVYYDVQAcrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 409
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 258-345 5.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 258 RGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 337
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                  ....*...
gi 1720422697 338 EDCVKALV 345
Cdd:PHA02875  181 IAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
325-381 6.73e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 6.73e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720422697 325 GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGnekGDTALHIAARWGYEGIIETLL 381
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 192-343 1.36e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 192 TPIDCLFKhiaSGN-QKEVERLL---SQDDQDKDA-MQKMCHPLC-SCEDCEKLIsgRLNDPSVVTPFSRDDRGQTPLHV 265
Cdd:PHA03095  154 TPLAVLLK---SRNaNVELLRLLidaGADVYAVDDrFRSLLHHHLqSFKPRARIV--RELIRAGCDPAATDMLGNTPLHS 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 266 AALCG--QASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKA 343
Cdd:PHA03095  229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
541-592 1.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720422697 541 SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL 592
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 588-660 1.84e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 1.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720422697 588 AKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFY 660
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 254-631 1.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.68  E-value: 1.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 254 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQK----------------GFQSVTLL------- 310
Cdd:PHA02876  173 AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidtikaiidnrsniNKNDLSLLkairned 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 311 ----LLHYKASTEVQ--DNNGNTPLHLACtygQEDCVKALVYYDVQ-ACRLDIGNEKGDTALHIAARWGYEGI-IETLLQ 382
Cdd:PHA02876  253 letsLLLYDAGFSVNsiDDCKNTPLHHAS---QAPSLSRLVPKLLErGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIM 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 383 NGAPTAVQNRLKETPLkcalnskilsimeaHHLSSDRRPRPSEVPAQSPTRSVDSisqgsstssfssisvsfrqeevkKD 462
Cdd:PHA02876  330 LGADVNAADRLYITPL--------------HQASTLDRNKDIVITLLELGANVNA-----------------------RD 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 463 YREVEKLLRAVADGDLEMVRYLLEWTEDdLDDVEDAISTVdLEFChpLCqcpkcapaqklarisanglsvnvtnqdGFSP 542
Cdd:PHA02876  373 YCDKTPIHYAAVRNNVVIINTLLDYGAD-IEALSQKIGTA-LHFA--LC---------------------------GTNP 421

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 543 lHMAalhgrtdlVPLLLKHGAYSGARNTSQAVPLHLACQQG-HFQVAKCLLDSNAKPNKKDLSGNTPLICACsaGHHEVA 621
Cdd:PHA02876  422 -YMS--------VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIV 490

                         410
                  ....*....|
gi 1720422697 622 ALLLQHGASI 631
Cdd:PHA02876  491 NILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 490-669 2.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 490 DDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARN 569
Cdd:PHA02878   21 EYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 570 TSQAVplHLACQQGHFQVAKCLLDSNAKPNKkdlSGNTPLICACSAG---HHEVAALLLQHGASINACN-NKGNTALHEA 645
Cdd:PHA02878  101 TLVAI--KDAFNNRNVEIFKIILTNRYKNIQ---TIDLVYIDKKSKDdiiEAEITKLLLSYGADINMKDrHKGNTALHYA 175

                         170       180
                  ....*....|....*....|....
gi 1720422697 646 VMGRHTLVVELLLFYGASVDILNK 669
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDK 199
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 212-314 2.36e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 212 LLSQDDQDKDAMQKMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYH 291
Cdd:PTZ00322   68 LTTEEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                          90       100
                  ....*....|....*....|...
gi 1720422697 292 GSTPLHLACQKGFQSVTLLLLHY 314
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 266-385 2.82e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 266 AALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPL---------------- 329
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 330 HLA------------CTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGA 385
Cdd:PLN03192  612 HFAsisdphaagdllCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 233-382 2.93e-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: 54.32  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 233 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 293
Cdd:TIGR00870  97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 294 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 359
Cdd:TIGR00870 177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                         170       180
                  ....*....|....*....|...
gi 1720422697 360 KGDTALHIAARWGYEGIIETLLQ 382
Cdd:TIGR00870 256 QGLTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
278-332 8.05e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 8.05e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422697 278 LVSKGAV-VNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 332
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 605-636 8.24e-07

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 46.13  E-value: 8.24e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720422697 605 GNTPLICAC-SAGHHEVAALLLQHGASINACNN 636
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
292-345 9.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 292 GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALV 345
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 259-383 1.43e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 259 GQTPLHVAALCGQASLIDFLVSKGAVVN---ATD-----------YHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 324
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 325 GNTPLHLACTygQEDCVKALVYYDV---------QACRLDIGNEKGDTALHIAARWGYEGIIETLLQN 383
Cdd:cd22192   169 GNTVLHILVL--QPNKTFACQMYDLilsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 255-358 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 255 RDDRGQTPLHVA-ALCGQASLIDFLVSKGAVVNATDY-HGSTPLHLACQKgfQSVTLLLLHYKASTEVQDNNGNTPLHLA 332
Cdd:PHA02878  230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                          90       100
                  ....*....|....*....|....*.
gi 1720422697 333 ctygqedcvkALVYYDVQACRLDIGN 358
Cdd:PHA02878  308 ----------VKQYLCINIGRILISN 323
Ank_5 pfam13857
Ankyrin repeats (many copies);
252-299 1.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.60e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422697 252 PFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA 299
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 258-381 1.79e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.68  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 258 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLlhYKASTEV-- 320
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720422697 321 QDNNGNTPLHLACTYG-----QEDCVKALvyYD--VQACR---LD-IGNEKGDTALHIAARWGYEGIIETLL 381
Cdd:cd22194   218 QDSRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 60-158 3.75e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.68  E-value: 3.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697   60 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 139
Cdd:smart00167   2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                           90
                   ....*....|....*....
gi 1720422697  140 AKDELGYCLTSVEAAIEYI 158
Cdd:smart00167  81 LTGEGGYYLTSLSAALALI 99
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 498-647 3.86e-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: 50.40  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 498 AISTVDLEFCHPLCQCPKCAPAQKLARisanglsvnvtnqdGFSPLHMAALHGRTDLVPLLLKhgaysGARN------TS 571
Cdd:cd22192    24 AAKENDVQAIKKLLKCPSCDLFQRGAL--------------GETALHVAALYDNLEAAVVLME-----AAPElvnepmTS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 572 Q----AVPLHLACQQGHFQVAKCLLDSNA------------KPNKKDLS--GNTPLICACSAGHHEVAALLLQHGASINA 633
Cdd:cd22192    85 DlyqgETALHIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                         170
                  ....*....|....
gi 1720422697 634 CNNKGNTALHEAVM 647
Cdd:cd22192   165 QDSLGNTVLHILVL 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
261-312 4.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720422697 261 TPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLL 312
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
310-368 4.99e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 4.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720422697 310 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQacrLDIGNEKGDTALHIA 368
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 605-633 6.71e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 6.71e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720422697  605 GNTPLICACSAGHHEVAALLLQHGASINA 633
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
525-579 9.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 9.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 525 ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA 579
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 591-665 9.70e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 9.70e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 591 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVD 665
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
Ank_5 pfam13857
Ankyrin repeats (many copies);
598-645 1.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422697 598 PNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEA 645
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 224-262 1.05e-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: 1.05e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720422697 224 QKMCHPLCSCEDCEKLISG-RLNDPSVVTPFSRDDRGQTP 262
Cdd:cd22886     3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 263-411 1.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 263 LHVAALC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 337
Cdd:PHA02875    1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 338 EDCVKALVyyDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIME 411
Cdd:PHA02875   81 VKAVEELL--DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 258-382 2.48e-05

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: 47.93  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 258 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD-------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEVQ 321
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 322 DNNGNTPLHlACTYGQEDCVK--ALV--YYD--VQA-CRLD-------IGNEKGDTALHIAARWGYEGIIETLLQ 382
Cdd:cd22197   173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDglLQAgARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 254-324 3.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720422697 254 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 324
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 258-382 3.36e-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: 47.49  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 258 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLL--HYKASTEV 320
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 321 QDNNGNTPLHLACTYG---QEDCVKALVYYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 382
Cdd:cd22196   173 RDSMGNTVLHALVEVAdntPENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
PHA02946 PHA02946
ankyin-like protein; Provisional
 591-665 6.98e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 6.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720422697 591 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVE---LLLFYGASVD 665
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKIN 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 637-669 7.01e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 7.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720422697 637 KGNTALHEAV-MGRHTLVVELLLFYGASVDILNK 669
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 212-398 1.58e-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: 45.39  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 212 LLSQDDQDKDAMQKmchpLCSCEDCEklisgrlndpsvvtPFSRDDRGQTPLHVAALCGQASLIDFLVSKG-AVVN--AT 288
Cdd:cd22192    22 LLAAKENDVQAIKK----LLKCPSCD--------------LFQRGALGETALHVAALYDNLEAAVVLMEAApELVNepMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 289 D--YHGSTPLHLACQKgfQSVTL--LLLHYKASTevqdnngNTPlhLACTYGQEDCVKALVYYdvqacrldignekGDTA 364
Cdd:cd22192    84 SdlYQGETALHIAVVN--QNLNLvrELIARGADV-------VSP--RATGTFFRPGPKNLIYY-------------GEHP 139

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720422697 365 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPL 398
Cdd:cd22192   140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 605-633 1.82e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.82e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720422697 605 GNTPLICACSAGHHEVAALLLQHGASINA 633
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 324-349 2.08e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.08e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720422697  324 NGNTPLHLACTYGQEDCVKALVYYDV 349
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02946 PHA02946
ankyin-like protein; Provisional
 251-355 2.09e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 251 TPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLAC---QKGFQSVTLLLLHYKASTEVQDNNGNT 327
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                          90       100
                  ....*....|....*....|....*...
gi 1720422697 328 PLhLACTYGQEDCVKALVYYDVQACRLD 355
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEARIVD 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
522-559 2.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.33e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720422697 522 LARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLL 559
Cdd:pfam13637  17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 456-623 2.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 456 QEEVKKDYREVEKLL---RAVADGDLEMVryllewTEDDLDDVEDAISTVDLefchplCQCPKCAPAQKLARISANGLSV 532
Cdd:PTZ00322   41 QEEIARIDTHLEALEateNKDATPDHNLT------TEEVIDPVVAHMLTVEL------CQLAASGDAVGARILLTGGADP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 533 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL---------DSNAKPNKKDL 603
Cdd:PTZ00322  109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKPDSFTG 188

                         170       180
                  ....*....|....*....|
gi 1720422697 604 SGNTPLICACSAGHHEVAAL 623
Cdd:PTZ00322  189 KPPSLEDSPISSHHPDFSAV 208
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 610-700 3.37e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 610 ICACSAGHHEVAA-LLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDS--KIME 686
Cdd:PTZ00322   86 LCQLAASGDAVGArILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQ 165

                          90
                  ....*....|....
gi 1720422697 687 LLQVVPGCVASLDS 700
Cdd:PTZ00322  166 LLSRHSQCHFELGA 179
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 258-289 3.55e-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: 3.55e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720422697 258 RGQTPLHVAAL-CGQASLIDFLVSKGAVVNATD 289
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 538-563 4.65e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.65e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720422697  538 DGFSPLHMAALHGRTDLVPLLLKHGA 563
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 538-563 6.51e-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: 6.51e-04
                          10        20
                  ....*....|....*....|....*.
gi 1720422697 538 DGFSPLHMAALHGRTDLVPLLLKHGA 563
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
361-402 7.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720422697 361 GDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCAL 402
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-398 9.23e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 310 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDignEKGDTALHIAARWGYEGIIETLLQ------- 382
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRhsqchfe 176

                          90       100
                  ....*....|....*....|..
gi 1720422697 383 ---NGAP---TAVQNRLKETPL 398
Cdd:PTZ00322  177 lgaNAKPdsfTGKPPSLEDSPI 198
Ank_5 pfam13857
Ankyrin repeats (many copies);
624-678 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720422697 624 LLQHG-ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 678
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 360-392 1.06e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720422697 360 KGDTALHIAA-RWGYEGIIETLLQNGAPTAVQNR 392
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 258-287 1.36e-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: 1.36e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720422697  258 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 287
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 360-385 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: 36.80  E-value: 1.43e-03
                           10        20
                   ....*....|....*....|....*.
gi 1720422697  360 KGDTALHIAARWGYEGIIETLLQNGA 385
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 253-367 1.60e-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: 42.17  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 253 FSRDDRGQTPLHVAAL---CGQASLIDFLV-------SKGAVVNA--TD--YHGSTPLHLACQKgfQSVTL--LLLHYKA 316
Cdd:cd21882    20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLeaapdsgNPKELVNApcTDefYQGQTALHIAIEN--RNLNLvrLLVENGA 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720422697 317 STEVQDNN-------------GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHI 367
Cdd:cd21882    98 DVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 575-600 2.05e-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: 2.05e-03
                           10        20
                   ....*....|....*....|....*.
gi 1720422697  575 PLHLACQQGHFQVAKCLLDSNAKPNK 600
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 538-569 2.08e-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: 36.50  E-value: 2.08e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720422697 538 DGFSPLHMAALH-GRTDLVPLLLKHGAYSGARN 569
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 507-544 2.45e-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: 36.46  E-value: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720422697 507 CHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLH 544
Cdd:cd22885     3 CHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 258-287 2.45e-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: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720422697 258 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 287
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 355-421 2.87e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 2.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 355 DIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSK---ILSIMeaHHLSSDRRP 421
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHFASISDP 619
Ank_2 pfam12796
Ankyrin repeats (3 copies);
365-412 3.08e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720422697 365 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 412
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 637-666 3.20e-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: 35.70  E-value: 3.20e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720422697 637 KGNTALHEAVMGRHTLVVELLLFYGASVDI 666
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 637-666 3.39e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.39e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720422697  637 KGNTALHEAVMGRHTLVVELLLFYGASVDI 666
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 324-347 3.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.51e-03
                          10        20
                  ....*....|....*....|....*
gi 1720422697 324 NGNTPLHLACT-YGQEDCVKALVYY 347
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 235-356 3.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 235 DCEKLISGRLNDPSVvtpfSRDDRgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLhy 314
Cdd:PHA02875  116 DIMKLLIARGADPDI----PNTDK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-- 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720422697 315 kastevqdNNGNTPLHlactYGQEDCVKALVyYDVQACRLDI 356
Cdd:PHA02875  189 --------DSGANIDY----FGKNGCVAALC-YAIENNKIDI 217
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 251-330 4.92e-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: 40.61  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 251 TPFsRD--DRGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHLA-CQKGFQSVTLLL-- 311
Cdd:cd22195   128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                          90
                  ....*....|....*....
gi 1720422697 312 LHYKASTEVQDNNGNTPLH 330
Cdd:cd22195   207 AHKKADLRRQDSRGNTVLH 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 324-349 5.34e-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: 5.34e-03
                          10        20
                  ....*....|....*....|....*.
gi 1720422697 324 NGNTPLHLACTYGQEDCVKALVYYDV 349
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 592-678 6.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422697 592 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDILNKR 670
Cdd:PHA02884   57 ADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTND 136


                  ....*...
gi 1720422697 671 QYTAADCA 678
Cdd:PHA02884  137 MVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 250-302 8.16e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 8.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720422697 250 VTPFSR-----------DDRGQTPLHVAALCGQA----SLIDFLVSKGAVVNATD-YHGSTPLHLACQK 302
Cdd:PHA02741   40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAHR 108
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 620-684 9.21e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 9.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720422697 620 VAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDSKI 684
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
 
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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