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Conserved domains on  [gi|1304473103|ref|NP_001345805|]
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ankyrin repeat domain-containing protein 27 isoform 3 [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];
708-878 6.39e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.28  E-value: 6.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  708 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 787
Cdd:COG0666     67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  788 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 867
Cdd:COG0666    147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                          170
                   ....*....|...
gi 1304473103  868 EQ--DSKIMELLQ 878
Cdd:COG0666    227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 4.57e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 4.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.66e-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: 1.66e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1304473103  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
VPS9 super family cl19569
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.23e-15

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


The actual alignment was detected with superfamily member pfam02204:

Pssm-ID: 473191  Cd Length: 104  Bit Score: 71.86  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1304473103  344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
708-878 6.39e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.28  E-value: 6.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  708 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 787
Cdd:COG0666     67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  788 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 867
Cdd:COG0666    147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                          170
                   ....*....|...
gi 1304473103  868 EQ--DSKIMELLQ 878
Cdd:COG0666    227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 4.57e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 4.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
Ank_2 pfam12796
Ankyrin repeats (3 copies);
765-857 5.02e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 5.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  765 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 844
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1304473103  845 LLLFYGASVDILN 857
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 7.68e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 7.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  500 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1304473103  580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.66e-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: 1.66e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1304473103  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 714-858 8.45e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  714 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 789
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  790 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 853
Cdd:PHA03100   172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                   ....*
gi 1304473103  854 DILNK 858
Cdd:PHA03100   252 KTIIE 256
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 691-731 1.86e-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: 1.86e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1304473103  691 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 731
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.23e-15

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


Pssm-ID: 460489  Cd Length: 104  Bit Score: 71.86  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1304473103  344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-622 1.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  520 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1304473103  597 ---LKETPLKCALNSKIL--SIMEAHHLSSD 622
Cdd:PHA03100   258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 462-586 9.07e-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: 55.96  E-value: 9.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 524
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304473103  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22193    155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 3.80e-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: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  437 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  498 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 1304473103  564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 5.60e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.29  E-value: 5.60e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1304473103   344 AKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 794-822 7.14e-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: 7.14e-06
                            10        20
                    ....*....|....*....|....*....
gi 1304473103   794 GNTPLICACSAGHHEVAALLLQHGASINA 822
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.28e-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: 2.28e-04
                            10        20
                    ....*....|....*....|....*.
gi 1304473103   528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
708-878 6.39e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.28  E-value: 6.39e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  708 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 787
Cdd:COG0666     67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  788 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 867
Cdd:COG0666    147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226

                          170
                   ....*....|...
gi 1304473103  868 EQ--DSKIMELLQ 878
Cdd:COG0666    227 AEngNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
716-867 4.15e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.19  E-value: 4.15e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  716 ANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGN 795
Cdd:COG0666    108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  796 TPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 867
Cdd:COG0666    188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
710-877 1.84e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  710 KLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNK 789
Cdd:COG0666     36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  790 KDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA-- 867
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAae 195

                          170
                   ....*....|
gi 1304473103  868 EQDSKIMELL 877
Cdd:COG0666    196 NGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-864 2.17e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.17e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  476 ASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVqa 555
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  556 cRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSImeahhlssdrrprpsevpaqsp 635
Cdd:COG0666     79 -DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI---------------------- 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  636 trsvdsisqgsstssfssisvsfrqeevkkdyreVRYLLEwteddlddvedaistvdlefchplcqcpkcapaqklaris 715
Cdd:COG0666    136 ----------------------------------VKLLLE---------------------------------------- 141

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  716 aNGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGN 795
Cdd:COG0666    142 -AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK 220

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304473103  796 TPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAA 864
Cdd:COG0666    221 TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 4.57e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 4.57e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    163 NGNLEIVKLLLEAGA---DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
459-616 5.58e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 5.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  459 RDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACT 538
Cdd:COG0666    116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  539 YGQEDCVKALVYYDVqacRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:COG0666    196 NGHLEIVKLLLEAGA---DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
457-831 3.74e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 3.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  457 FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:COG0666     48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  537 CTYGQEDCVKALVYY--DVqacrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAptavqnrlketplkcalnskilsim 614
Cdd:COG0666    128 AYNGNLEIVKLLLEAgaDV-----NAQDNDGNTPLHLAAANGNLEIVKLLLEAGA------------------------- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  615 eahhlssdrrprpsevpaqsptrsvdsisqgsstssfssisvsfrqeevkkdyrevryllewteddlddvedaistvdle 694
Cdd:COG0666        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  695 fchplcqcpkcapaqklarisanglSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHF 774
Cdd:COG0666    178 -------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1304473103  775 QVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTAL 831
Cdd:COG0666    233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
708-877 1.93e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  708 AQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKP 787
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  788 NKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA---A 864
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPlhlA 160

                          170
                   ....*....|...
gi 1304473103  865 dCAEQDSKIMELL 877
Cdd:COG0666    161 -AANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
765-857 5.02e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 5.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  765 LHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHgASINACNNkGNTALHEAVMGRHTLVVE 844
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1304473103  845 LLLFYGASVDILN 857
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
732-822 2.13e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 2.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  732 LHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDsNAKPNKKDlSGNTPLICACSAGHHEVAA 811
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1304473103  812 LLLQHGASINA 822
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
500-589 7.68e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 7.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  500 LHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdvqaCRLDIGNEkGDTALHIAARWGYEG 579
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1304473103  580 IIETLLQNGA 589
Cdd:pfam12796   76 IVKLLLEKGA 85
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-468 1.66e-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: 1.66e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1304473103  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLH 468
Cdd:cd22885      1 KLCHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 714-858 8.45e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 8.45e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  714 ISANGLSVNVTNQDGFSPLHMAALH--GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 789
Cdd:PHA03100    92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  790 K----------------DLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASV 853
Cdd:PHA03100   172 KnrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                   ....*
gi 1304473103  854 DILNK 858
Cdd:PHA03100   252 KTIIE 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
467-559 1.47e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  467 LHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEvqDNNGNTPLHLACTYGQEDCVK 546
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1304473103  547 ALVYYDVQACRLD 559
Cdd:pfam12796   79 LLLEKGADINVKD 91
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 691-731 1.86e-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: 1.86e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1304473103  691 VDLEFCHPLCQCPKCAPAQK-LARISANGLSVNVTNQDGFSP 731
Cdd:cd22886      1 SDPELCHPLCQCDKCAPLQKrTARLPKSGLNVNSCNSDGFTP 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 722-856 7.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 7.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  722 NVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICA 801
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1304473103  802 CSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDIL 856
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
VPS9 pfam02204
Vacuolar sorting protein 9 (VPS9) domain; This domain acts as a GDP-GTP exchange factor (GEF). ...
 264-363 4.23e-15

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


Pssm-ID: 460489  Cd Length: 104  Bit Score: 71.86  E-value: 4.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNLETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:pfam02204    1 WEQAQQELKKLNEAKSPREKLKCLLRTCKLITEALSKSNRDESLGADDLLPILIYVLIRANPPNLYSNLQFISEFRDPDL 80

                           90       100
                   ....*....|....*....|
gi 1304473103  344 AKDELGYCLTSVEAAIEYIR 363
Cdd:pfam02204   81 LSGEEGYYLTTLEAALEFIE 100
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 716-857 1.00e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 1.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  716 ANGLSVNVTNQD-GFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSG 794
Cdd:PHA02878   155 SYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG 234

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  795 NTPL-ICACSAGHHEVAALLLQHGASINACNN-KGNTALHEAVmgRHTLVVELLLFYGASVDILN 857
Cdd:PHA02878   235 NTPLhISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLN 297
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 460-622 1.55e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.01  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  460 DDRGQTPLHVAALC--GQASLIDFLVSKGAVVNATDYHGSTPLHLA---CQKGFQSVTLLLLH---------------YK 519
Cdd:PHA03100   103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDLKILKLLIDKgvdinaknrvnyllsYG 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  520 ASTEVQDNNGNTPLHLACTYGQEDCVKALVYY--DVQACrldigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNR- 596
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgaNPNLV-----NKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIEt 257

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1304473103  597 ---LKETPLKCALNSKIL--SIMEAHHLSSD 622
Cdd:PHA03100   258 llyFKDKDLNTITKIKMLkkSIMYMFLLDPG 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 387-607 1.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  387 MNLLSQMTSTPidcLFKHIASGNQKEVERLLSQDDQDKDAMQKMCHPLCSC-----EDCEKLISGRLNDPSV-------- 453
Cdd:PHA02874    28 INISVDETTTP---LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigaHDIIKLLIDNGVDTSIlpipciek 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  454 ----------VTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTE 523
Cdd:PHA02874   105 dmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  524 VQDNNGNTPLHLACTYGQEDCVKALVyydVQACRLDIGNEKGDTALHIAARWGYEGIieTLLQNGAPTAVQNRLKETPLK 603
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLH 259


                   ....
gi 1304473103  604 CALN 607
Cdd:PHA02874   260 HAIN 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 461-606 1.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  461 DRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYg 540
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY- 244

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304473103  541 qedcvkaLVYYDVQACRLDIG---NEK----GDTALHIAARwgYEGIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:PHA02878   245 -------CKDYDILKLLLEHGvdvNAKsyilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 480-853 1.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  480 DFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVyydvqACRLD 559
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII-----DNRSN 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  560 IgnEKGDTALHIAARwgYEGIIETLLQNGAPTAVQ--NRLKETPLKCALNSKILSIMEAHHLSSDRRPRPSEVPAQSPtr 637
Cdd:PHA02876   237 I--NKNDLSLLKAIR--NEDLETSLLLYDAGFSVNsiDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP-- 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  638 svdsisqgsstssfssisvSFRQEEVKKDYREVRYLLEWTEDdlddvedaISTVDLEFCHPLCQcpkcapAQKLAR---- 713
Cdd:PHA02876   311 -------------------LYLMAKNGYDTENIRTLIMLGAD--------VNAADRLYITPLHQ------ASTLDRnkdi 357

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  714 -ISANGLSVNVTNQDGF--SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA-CQQGHFQVAKCLLDSNAKPNK 789
Cdd:PHA02876   358 vITLLELGANVNARDYCdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNS 437

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  790 KDLSGNTPLICACSAG-HHEVAALLLQHGASINACNNKGNTALHEAvMGRHTlVVELLLFYGASV 853
Cdd:PHA02876   438 KNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA-LEYHG-IVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 711-862 1.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  711 LARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNK- 789
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDv 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  790 --KDlsGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYT 862
Cdd:PHA02875    98 fyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 713-861 2.35e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  713 RISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQ-----VAKCLLDSNAKP 787
Cdd:PHA03100    20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  788 NKKDLSGNTPLICACSA--GHHEVAALLLQHGASINACNNKGNTALHEAVMGRH--TLVVELLLFYGASVDILNKRQY 861
Cdd:PHA03100   100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-791 2.40e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 2.40e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  717 NGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAysGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKD 791
Cdd:pfam12796   19 NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 718-872 3.05e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.07  E-value: 3.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  718 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTP 797
Cdd:PHA02874   114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  798 LICACSAGHHEVAALLLQHGASI-NACNNkGNTALHEAVMGRHTlVVELL--------------------LFYGASVDIL 856
Cdd:PHA02874   194 LHNAAEYGDYACIKLLIDHGNHImNKCKN-GFTPLHNAIIHNRS-AIELLinnasindqdidgstplhhaINPPCDIDII 271

                          170
                   ....*....|....*.
gi 1304473103  857 NKRQYTAADCAEQDSK 872
Cdd:PHA02874   272 DILLYHKADISIKDNK 287
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 429-466 3.57e-13

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


Pssm-ID: 439264 [Multi-domain]  Cd Length: 38  Bit Score: 64.58  E-value: 3.57e-13
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1304473103  429 KMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 711-858 3.78e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  711 LARISANGLSVNVTNQDGFSPLHM---AALHGRTDLVPLLLKHGAYSGARNTSQAVPLHL-ACQQGHFQVAKCLLDSNAK 786
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGAD 109

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  787 PNKKDLSGNTPL-ICACS-AGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVELL-LFYGASVDILNK 858
Cdd:PHA03095   110 VNAKDKVGRTPLhVYLSGfNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSRNANVELLrLLIDAGADVYAV 183
PHA03095 PHA03095
ankyrin-like protein; Provisional
 482-854 3.95e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 3.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  482 LVSKGAVVNATDYHGSTPLHLACQKGFQSVT---LLLLHYKASTEVQDNNGNTPLHLACTYGQ-EDCVKALVYY--DVQA 555
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgaDVNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  556 CrldigNEKGDTALHIAAR--WGYEGIIETLLQNGA-PTAVQNRLKeTPLKCALNSKILSImeahhlssdrrprpsEVpa 632
Cdd:PHA03095   113 K-----DKVGRTPLHVYLSgfNINPKVIRLLLRKGAdVNALDLYGM-TPLAVLLKSRNANV---------------EL-- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  633 qsptrsvdsisqgsstssfssisvsfrqeevkkdyreVRYLLEWTEDdlddvedaISTVDLEF---CHPLCQCPKcAPAQ 709
Cdd:PHA03095   170 -------------------------------------LRLLIDAGAD--------VYAVDDRFrslLHHHLQSFK-PRAR 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  710 KLARISANGLSVNVTNQDGFSPLHMAALHG---RTDLVPLLLKhGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAK 786
Cdd:PHA03095   204 IVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  787 PNKKDLSGNTPLICACSAGHHE-VAALLLQH------GASINACNNKGNTALHEAvmgRHTLVVELLLFYGASVD 854
Cdd:PHA03095   283 INAVSSDGNTPLSLMVRNNNGRaVRAALAKNpsaetvAATLNTASVAGGDIPSDA---TRLCVAKVVLRGAFSLL 354
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 478-613 5.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 5.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  478 LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL--LLLHYKASTEVQDNNGNTPLHLA--CTYGQEDCVKALVY--Y 551
Cdd:PHA03100    88 IVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIveYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDkgV 167

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304473103  552 DVQA-----------CRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 613
Cdd:PHA03100   168 DINAknrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 742-866 1.03e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  742 DLVPLLLKHGA---YSGARNTSqavPLHLACQQGHFQVAK---CLLDSNAKPNKKDLSGNTPLIC-ACSAGHHEVAALLL 814
Cdd:PHA03095    28 EEVRRLLAAGAdvnFRGEYGKT---PLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLI 104

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1304473103  815 QHGASINACNNKGNTALHE--AVMGRHTLVVELLLFYGASVDILNKRQYTAADC 866
Cdd:PHA03095   105 KAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
794-847 1.77e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.77e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1304473103  794 GNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLL 847
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 460-551 4.08e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 4.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  460 DDRGQTPLHVAA--LC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTP 532
Cdd:PTZ00322    72 EVIDPVVAHMLTveLCqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP 151

                           90
                   ....*....|....*....
gi 1304473103  533 LHLACTYGQEDCVKALVYY 551
Cdd:PTZ00322   152 LELAEENGFREVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
456-526 5.16e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.16e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKgAVVNATDYhGSTPLHLACQKGFQSVTLLLLHYKASTEVQD 526
Cdd:pfam12796   23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 741-892 3.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 3.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  741 TDLVPLLLKHGAYSGARNTSQ-AVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGAS 819
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1304473103  820 INACNNKGNTALHEAVmGR--HTLVVELLLFYGASVDILNK-RQYTAADCAEQDSKIMELLQVVPGCVASLDSVEE 892
Cdd:PHA02878   227 TDARDKCGNTPLHISV-GYckDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADINSLNSYKL 301
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-608 3.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 3.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  475 QASLIDFLVSKGAVVNATDYH-GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYdv 553
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-- 223

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  554 qACRLDIGNEKGDTALHIAARW--GYEgIIETLLQNGAPTAVQNRLKE-TPLKCALNS 608
Cdd:PHA02878   224 -GASTDARDKCGNTPLHISVGYckDYD-ILKLLLEHGVDVNAKSYILGlTALHSSIKS 279
PHA02798 PHA02798
ankyrin-like protein; Provisional
 741-866 4.97e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.32  E-value: 4.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  741 TDLVPLLLKHGAYSGARNTSQAVPL-----HLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGH---HEVAAL 812
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  813 LLQHGASINACNNKGNTALHEAVMGRHTL---VVELLLFYGASVDIL-NKRQYTAADC 866
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHnNKEKYDTLHC 188
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 707-838 6.13e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 6.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  707 PAQKLAR-ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQ-GHFQVAKCLLDSN 784
Cdd:PHA02878   179 KDQRLTElLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  785 AKPNKKD-LSGNTPLicACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGR 838
Cdd:PHA02878   259 VDVNAKSyILGLTAL--HSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 718-863 2.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  718 GLSVNVTNQDGFSPLHMAA-LHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGH-FQVAKCLLDSNAKPNKKDLSGN 795
Cdd:PHA02876   263 GFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI 342

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304473103  796 TPLICACSAGHH-EVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTA 863
Cdd:PHA02876   343 TPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTA 411
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 531-846 3.38e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 3.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  531 TPLHLACTYGQEDCVKALVYYDVQACRLdigNEKGDTALHIAARWGYEGIIETLLQNGAPTAVqnrlkeTPLKCALNSKI 610
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHI---NTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI------LPIPCIEKDMI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  611 LSIMEAHhLSSDRRPRPSEVpaqsptrsvdsisqgsstssfssisvsFRQEEVKK-DYREVRYLLEWTEDdlddvedaIS 689
Cdd:PHA02874   108 KTILDCG-IDVNIKDAELKT---------------------------FLHYAIKKgDLESIKMLFEYGAD--------VN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  690 TVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLAC 769
Cdd:PHA02874   152 IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  770 QqgHFQVAKCLLDSNAKPNKKDLSGNTPLICA----CSAghhEVAALLLQHGASINACNNKGNTALHEAV--MGRHTLVV 843
Cdd:PHA02874   232 I--HNRSAIELLINNASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIK 306


                   ...
gi 1304473103  844 ELL 846
Cdd:PHA02874   307 DII 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 722-816 3.38e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  722 NVTNQDGFSP--LHMAALH-------GRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDL 792
Cdd:PTZ00322    67 NLTTEEVIDPvvAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146

                           90       100
                   ....*....|....*....|....
gi 1304473103  793 SGNTPLICACSAGHHEVAALLLQH 816
Cdd:PTZ00322   147 DGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 742-862 3.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 3.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  742 DLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASIN 821
Cdd:PHA02874   105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1304473103  822 ACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYT 862
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 716-821 4.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 4.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  716 ANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKDLSGN 795
Cdd:PHA02875   123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                           90       100
                   ....*....|....*....|....*..
gi 1304473103  796 TPLIC-ACSAGHHEVAALLLQHGASIN 821
Cdd:PHA02875   203 VAALCyAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 718-857 5.79e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 5.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  718 GLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLLDSNAKPNKKdlSGNTP 797
Cdd:PLN03192   548 KLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDL 625

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  798 LICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILN 857
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
764-814 7.20e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  764 PLHLACQQGHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLL 814
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKRD27_zf cd22883
Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 694-731 2.75e-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: 2.75e-08
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1304473103  694 EFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSP 731
Cdd:cd22883      1 EFCHPLCQCPKCAPAVSRLAKDPSGVGVNSRDQDGRTP 38
PHA03095 PHA03095
ankyrin-like protein; Provisional
 716-855 3.85e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 3.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  716 ANGLSVNVTNQDGFSPLHmaALHGRTD----LVPLLLKHGAYSGARNTSQAVPLHLACQQGH--FQVAKCLLDSNAKPNK 789
Cdd:PHA03095   140 RKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAA 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  790 KDLSGNTPL-----ICACSAGHheVAALLLqHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDI 855
Cdd:PHA03095   218 TDMLGNTPLhsmatGSSCKRSL--VLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 461-545 6.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 6.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  461 DRGQTPLHVAALCGQaSLIDFLVSKgAVVNATDYHGSTPLHLA----CQKgfqSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:PHA02874   221 KNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAinppCDI---DIIDILLYHKADISIKDNKGENPIDTA 295


                   ....*....
gi 1304473103  537 CTYGQEDCV 545
Cdd:PHA02874   296 FKYINKDPV 304
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 463-613 6.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  463 GQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKG-FQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  542 EDCVKALVYYDVQAcrlDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSI 613
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-549 6.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180


                   ....*...
gi 1304473103  542 EDCVKALV 549
Cdd:PHA02875   181 IAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
529-585 8.93e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 8.93e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1304473103  529 GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGnekGDTALHIAARWGYEGIIETLL 585
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 462-586 9.07e-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: 55.96  E-value: 9.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEV 524
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLaACTNQPDIVQYLLenEHQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1304473103  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22193    155 QDSRGNTVLHALVTVAdntkeNTKFVTRM--YDmilIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 396-547 1.41e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  396 TPIDCLFKhiaSGN-QKEVERLL---SQDDQDKDA-MQKMCHPLC-SCEDCEKLIsgRLNDPSVVTPFSRDDRGQTPLHV 469
Cdd:PHA03095   154 TPLAVLLK---SRNaNVELLRLLidaGADVYAVDDrFRSLLHHHLqSFKPRARIV--RELIRAGCDPAATDMLGNTPLHS 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  470 AALCG--QASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKA 547
Cdd:PHA03095   229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
730-781 1.90e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.90e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  730 SPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLACQQGHFQVAKCLL 781
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 777-849 2.31e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.31e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1304473103  777 AKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFY 849
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 416-518 2.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  416 LLSQDDQDKDAMQKMCHPLCSCEDCEKLISGRLNDPSVVTPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYH 495
Cdd:PTZ00322    68 LTTEEVIDPVVAHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147

                           90       100
                   ....*....|....*....|...
gi 1304473103  496 GSTPLHLACQKGFQSVTLLLLHY 518
Cdd:PTZ00322   148 GKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 679-858 2.96e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  679 DDLDDVEDAISTVDLEFCHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARN 758
Cdd:PHA02878    21 EYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  759 TSQAVplHLACQQGHFQVAKCLLDSNAKPNKkdlSGNTPLICACSAG---HHEVAALLLQHGASINACN-NKGNTALHEA 834
Cdd:PHA02878   101 TLVAI--KDAFNNRNVEIFKIILTNRYKNIQ---TIDLVYIDKKSKDdiiEAEITKLLLSYGADINMKDrHKGNTALHYA 175

                          170       180
                   ....*....|....*....|....
gi 1304473103  835 VMGRHTLVVELLLFYGASVDILNK 858
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDK 199
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 470-589 3.66e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  470 AALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPL---------------- 533
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  534 HLA------------CTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:PLN03192   612 HFAsisdphaagdllCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 437-586 3.80e-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: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  437 CEDC----EKLISGRLNDPSVVTP-FSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNA------------TD--YHGS 497
Cdd:TIGR00870   97 VEAIllhlLAAFRKSGPLELANDQyTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsfYHGE 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  498 TPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLAC----------TYGQEdCVKALVYYDVQACRL----DIGNE 563
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeELSCQ-MYNFALSLLDKLRDSkeleVILNH 255

                          170       180
                   ....*....|....*....|...
gi 1304473103  564 KGDTALHIAARWGYEGIIETLLQ 586
Cdd:TIGR00870  256 QGLTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
482-536 7.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 7.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1304473103  482 LVSKGAV-VNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 794-825 7.58e-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: 46.51  E-value: 7.58e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1304473103  794 GNTPLICAC-SAGHHEVAALLLQHGASINACNN 825
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 458-606 8.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 8.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  458 SRDDRGQTPLHVAALCGQAS-LIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTL-LLLHYKASTEVQDNNGNTPLHL 535
Cdd:PHA02876   268 SIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIrTLIMLGADVNAADRLYITPLHQ 347

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  536 ACTYGQ-EDCVKALVYYDVQACRLDIGNEkgdTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:PHA02876   348 ASTLDRnKDIVITLLELGANVNARDYCDK---TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 465-606 1.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  465 TPLHvaalcgQASLID-------FLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLA- 536
Cdd:PHA02876   343 TPLH------QASTLDrnkdiviTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAl 416

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  537 CTYGQEDCVKALVYydvQACRLDIGNEKGDTALHIAARWGYE-GIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:PHA02876   417 CGTNPYMSVKTLID---RGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL 484
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-549 1.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.28e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1304473103  496 GSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALV 549
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
456-503 1.54e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.54e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1304473103  456 PFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLA 503
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 463-587 1.84e-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: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  463 GQTPLHVAALCGQASLIDFLVSKGAVVN---ATD-----------YHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 528
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  529 GNTPLHLACTygQEDCVKALVYYDV---------QACRLDIGNEKGDTALHIAARWGYEGIIETLLQN 587
Cdd:cd22192    169 GNTVLHILVL--QPNKTFACQMYDLilsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-562 1.94e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  459 RDDRGQTPLHVA-ALCGQASLIDFLVSKGAVVNATDY-HGSTPLHLACQKgfQSVTLLLLHYKASTEVQDNNGNTPLHLA 536
Cdd:PHA02878   230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                           90       100
                   ....*....|....*....|....*.
gi 1304473103  537 ctygqedcvkALVYYDVQACRLDIGN 562
Cdd:PHA02878   308 ----------VKQYLCINIGRILISN 323
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 462-585 3.09e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.30  E-value: 3.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLlhYKASTEV-- 524
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLALaACTNQPEIVQLLM--EKESTDIts 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  525 QDNNGNTPLHLACTYG-----QEDCVKALvyYD--VQACR---LD-IGNEKGDTALHIAARWGYEGIIETLL 585
Cdd:cd22194    218 QDSRGNTVLHALVTVAedsktQNDFVKRM--YDmiLLKSEnknLEtIRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
514-572 4.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1304473103  514 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQacrLDIGNEKGDTALHIA 572
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 687-836 4.97e-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: 4.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  687 AISTVDLEFCHPLCQCPKCAPAQKLARisanglsvnvtnqdGFSPLHMAALHGRTDLVPLLLKhgaysGARN------TS 760
Cdd:cd22192     24 AAKENDVQAIKKLLKCPSCDLFQRGAL--------------GETALHVAALYDNLEAAVVLME-----AAPElvnepmTS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  761 Q----AVPLHLACQQGHFQVAKCLLDSNA------------KPNKKDLS--GNTPLICACSAGHHEVAALLLQHGASINA 822
Cdd:cd22192     85 DlyqgETALHIAVVNQNLNLVRELIARGAdvvspratgtffRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|....
gi 1304473103  823 CNNKGNTALHEAVM 836
Cdd:cd22192    165 QDSLGNTVLHILVL 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-516 5.38e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1304473103  465 TPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLL 516
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
VPS9 smart00167
Domain present in VPS9; Domain present in yeast vacuolar sorting protein 9 and other proteins.
 264-362 5.60e-06

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


Pssm-ID: 128469  Cd Length: 117  Bit Score: 46.29  E-value: 5.60e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103   264 IPRAKRELGQLNKCTSPQQKLLCLRKVVQLMTQSPSQRVNlETMCADDLLSVLLYLLVKTEIPNWMANLSYIKNFRFSSS 343
Cdd:smart00167    2 VEIEQIELKFLQLYKSPSDKIKCLLRACKLIYTLLETQSG-EVAGADDFLPVLIYVIIKCDPRDLLLNAEYMEEFLEPSL 80

                            90
                    ....*....|....*....
gi 1304473103   344 AKDELGYCLTSVEAAIEYI 362
Cdd:smart00167   81 LTGEGGYYLTSLSAALALI 99
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 794-822 7.14e-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: 7.14e-06
                            10        20
                    ....*....|....*....|....*....
gi 1304473103   794 GNTPLICACSAGHHEVAALLLQHGASINA 822
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
714-768 8.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 8.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  714 ISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGARNTSQAVPLHLA 768
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
787-834 9.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.62e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1304473103  787 PNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEA 834
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANKRD27_zf2 cd22886
second Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and ...
 428-466 1.24e-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: 1.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1304473103  428 QKMCHPLCSCEDCEKLISG-RLNDPSVVTPFSRDDRGQTP 466
Cdd:cd22886      3 PELCHPLCQCDKCAPLQKRtARLPKSGLNVNSCNSDGFTP 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 780-854 1.25e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  780 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVD 854
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD 618
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 467-615 1.70e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  467 LHVAALC-----GQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNNGNTPLHLACTYGQ 541
Cdd:PHA02875     1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304473103  542 EDCVKALVyyDVQACRLDIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIME 615
Cdd:PHA02875    81 VKAVEELL--DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 458-528 3.85e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.85e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  458 SRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLHYKASTEVQDNN 528
Cdd:PHA03100   187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 462-586 4.22e-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: 47.54  E-value: 4.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD-------------YHGSTPLHL-ACQKGFQSVTLLL--LHYKASTEVQ 525
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLaACTKQWDVVNYLLenPHQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  526 DNNGNTPLHlACTYGQEDCVK--ALV--YYD--VQA-CRLD-------IGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22197    173 DSLGNTVLH-ALVMIADNSPEnsALVikMYDglLQAgARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHILQ 246
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 462-586 4.31e-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: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHL-ACQKGFQSVTLLLL--HYKASTEV 524
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLaACTNQLDIVKFLLEnpHSPADISA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  525 QDNNGNTPLHLACTYG---QEDCVKALVYYD---VQACRL-------DIGNEKGDTALHIAARWGYEGIIETLLQ 586
Cdd:cd22196    173 RDSMGNTVLHALVEVAdntPENTKFVTKMYNeilILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILG 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 826-858 6.45e-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: 6.45e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1304473103  826 KGNTALHEAV-MGRHTLVVELLLFYGASVDILNK 858
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 780-854 8.05e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 8.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1304473103  780 LLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHeAVMGRHTLVVE---LLLFYGASVD 854
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKIN 134
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 416-602 2.02e-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: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  416 LLSQDDQDKDAMQKmchpLCSCEDCEklisgrlndpsvvtPFSRDDRGQTPLHVAALCGQASLIDFLVSKG-AVVN--AT 492
Cdd:cd22192     22 LLAAKENDVQAIKK----LLKCPSCD--------------LFQRGALGETALHVAALYDNLEAAVVLMEAApELVNepMT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  493 D--YHGSTPLHLACQKgfQSVTL--LLLHYKASTevqdnngNTPlhLACTYGQEDCVKALVYYdvqacrldignekGDTA 568
Cdd:cd22192     84 SdlYQGETALHIAVVN--QNLNLvrELIARGADV-------VSP--RATGTFFRPGPKNLIYY-------------GEHP 139

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1304473103  569 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPL 602
Cdd:cd22192    140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 794-822 2.22e-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: 2.22e-04
                           10        20
                   ....*....|....*....|....*....
gi 1304473103  794 GNTPLICACSAGHHEVAALLLQHGASINA 822
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 528-553 2.28e-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: 2.28e-04
                            10        20
                    ....*....|....*....|....*.
gi 1304473103   528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02946 PHA02946
ankyin-like protein; Provisional
 455-559 2.36e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  455 TPFSRDDRGQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLAC---QKGFQSVTLLLLHYKASTEVQDNNGNT 531
Cdd:PHA02946    64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgtdDEVIERINLLVQYGAKINNSVDEEGCG 143

                           90       100
                   ....*....|....*....|....*...
gi 1304473103  532 PLhLACTYGQEDCVKALVYYDVQACRLD 559
Cdd:PHA02946   144 PL-LACTDPSERVFKKIMSIGFEARIVD 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
711-748 2.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.94e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1304473103  711 LARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLL 748
Cdd:pfam13637   17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-493 3.39e-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: 38.81  E-value: 3.39e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1304473103  462 RGQTPLHVAAL-CGQASLIDFLVSKGAVVNATD 493
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 677-812 3.63e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  677 TEDDLDDVEDAISTVDLefchplCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLHMAALHGRTDLVPLLLKHGAYSGA 756
Cdd:PTZ00322    70 TEEVIDPVVAHMLTVEL------CQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1304473103  757 RNTSQAVPLHLACQQGHFQVAKCLL---------DSNAKPNKKDLSGNTPLICACSAGHHEVAAL 812
Cdd:PTZ00322   144 LDKDGKTPLELAEENGFREVVQLLSrhsqchfelGANAKPDSFTGKPPSLEDSPISSHHPDFSAV 208
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 799-889 3.95e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  799 ICACSAGHHEVAA-LLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCAEQDS--KIME 875
Cdd:PTZ00322    86 LCQLAASGDAVGArILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfrEVVQ 165

                           90
                   ....*....|....
gi 1304473103  876 LLQVVPGCVASLDS 889
Cdd:PTZ00322   166 LLSRHSQCHFELGA 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 727-752 5.10e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.10e-04
                            10        20
                    ....*....|....*....|....*.
gi 1304473103   727 DGFSPLHMAALHGRTDLVPLLLKHGA 752
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 727-752 7.95e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 7.95e-04
                           10        20
                   ....*....|....*....|....*.
gi 1304473103  727 DGFSPLHMAALHGRTDLVPLLLKHGA 752
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
Ank_4 pfam13637
Ankyrin repeats (many copies);
565-606 9.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 9.12e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1304473103  565 GDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCAL 606
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
813-867 9.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.87e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1304473103  813 LLQHG-ASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDILNKRQYTAADCA 867
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 564-596 1.01e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1304473103  564 KGDTALHIAA-RWGYEGIIETLLQNGAPTAVQNR 596
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 514-627 1.06e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  514 LLLHYKASTEVQDNNGNTPLHLACTYGQEDCVKALVYYDVQACRLDignEKGDTALHIAARWGYEGIIETLLQ------- 586
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD---KDGKTPLELAEENGFREVVQLLSRhsqchfe 176

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1304473103  587 ---NGAP---TAVQNRLKETPLKcalnskilsimeAHHLSSDRRPRP 627
Cdd:PTZ00322   177 lgaNAKPdsfTGKPPSLEDSPIS------------SHHPDFSAVPQP 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 462-491 1.46e-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: 1.46e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1304473103   462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 564-589 1.46e-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: 1.46e-03
                            10        20
                    ....*....|....*....|....*.
gi 1304473103   564 KGDTALHIAARWGYEGIIETLLQNGA 589
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 727-758 2.03e-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: 2.03e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1304473103  727 DGFSPLHMAALH-GRTDLVPLLLKHGAYSGARN 758
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 457-571 2.04e-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: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  457 FSRDDRGQTPLHVAAL---CGQASLIDFLV-------SKGAVVNA--TD--YHGSTPLHLACQKgfQSVTL--LLLHYKA 520
Cdd:cd21882     20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLeaapdsgNPKELVNApcTDefYQGQTALHIAIEN--RNLNLvrLLVENGA 97

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1304473103  521 STEVQDNN-------------GNTPLHLACTYGQEDCVKALVYYDVQACRLDIGNEKGDTALHI 571
Cdd:cd21882     98 DVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 764-789 2.25e-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: 2.25e-03
                            10        20
                    ....*....|....*....|....*.
gi 1304473103   764 PLHLACQQGHFQVAKCLLDSNAKPNK 789
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 462-491 3.03e-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: 3.03e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1304473103  462 RGQTPLHVAALCGQASLIDFLVSKGAVVNA 491
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANKRD27_zf1 cd22885
first Zn-fingernail found in ankyrin repeat domain-containing protein 27 (ANKRD27) and similar ...
 696-733 3.09e-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: 3.09e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1304473103  696 CHPLCQCPKCAPAQKLARISANGLSVNVTNQDGFSPLH 733
Cdd:cd22885      3 CHPLCSCDKCEKLLSGNRNDPSAVTVYSRDDRGYTALH 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-551 3.32e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.32e-03
                           10        20
                   ....*....|....*....|....*
gi 1304473103  528 NGNTPLHLACT-YGQEDCVKALVYY 551
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSK 25
Ank_2 pfam12796
Ankyrin repeats (3 copies);
569-616 3.35e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 3.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1304473103  569 LHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSKILSIMEA 616
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL 48
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 826-855 3.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.61e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1304473103   826 KGNTALHEAVMGRHTLVVELLLFYGASVDI 855
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 559-625 3.66e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 3.66e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  559 DIGNEKGDTALHIAARWGYEGIIETLLQNGAPTAVQNRLKETPLKCALNSK---ILSIMeaHHLSSDRRP 625
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKhhkIFRIL--YHFASISDP 619
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 826-855 3.91e-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: 3.91e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1304473103  826 KGNTALHEAVMGRHTLVVELLLFYGASVDI 855
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 439-560 4.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  439 DCEKLISGRLNDPSVvtpfSRDDRgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQKGFQSVTLLLLhy 518
Cdd:PHA02875   116 DIMKLLIARGADPDI----PNTDK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL-- 188

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1304473103  519 kastevqdNNGNTPLHlactYGQEDCVKALVyYDVQACRLDI 560
Cdd:PHA02875   189 --------DSGANIDY----FGKNGCVAALC-YAIENNKIDI 217
PHA02946 PHA02946
ankyin-like protein; Provisional
 431-535 5.30e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 5.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  431 CHPLCSCEDCEKLISGRLN----DPSVVTPFSRDdrgQTPLHVAALCGQASLIDFLVSKGAVVNATDYHGSTPLHLACQK 506
Cdd:PHA02946   142 CGPLLACTDPSERVFKKIMsigfEARIVDKFGKN---HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSK 218

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1304473103  507 GFQSVTLLLLhYKASTEVQDNN--GNTPLHL 535
Cdd:PHA02946   219 TVKNVDIINL-LLPSTDVNKQNkfGDSPLTL 248
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 455-534 6.25e-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: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  455 TPFsRD--DRGQTPLHVAALCGQASLIDFLVSKGAVVNATD--------------YHGSTPLHLA-CQKGFQSVTLLL-- 515
Cdd:cd22195    128 SPF-RDvyYRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyfYFGELPLSLAaCTNQPDIVHYLTen 206

                           90
                   ....*....|....*....
gi 1304473103  516 LHYKASTEVQDNNGNTPLH 534
Cdd:cd22195    207 AHKKADLRRQDSRGNTVLH 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 528-553 6.52e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 1304473103  528 NGNTPLHLACTYGQEDCVKALVYYDV 553
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 796-856 8.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 8.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1304473103  796 TPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGASVDIL 856
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 772-877 8.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 8.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  772 GHFQVAKCLLDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGNTALHEAVMGRHTLVVELLLFYGA 851
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100
                   ....*....|....*....|....*....
gi 1304473103  852 SV-DILNKRQYTAADCAE--QDSKIMELL 877
Cdd:PHA02875    93 FAdDVFYKDGMTPLHLATilKKLDIMKLL 121
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 781-867 8.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1304473103  781 LDSNAKPNKKDLSGNTPLICACSAGHHEVAALLLQHGASINACNNKGN-TALHEAVMGRHTLVVELLLFYGASVDILNKR 859
Cdd:PHA02884    57 ADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTND 136


                   ....*...
gi 1304473103  860 QYTAADCA 867
Cdd:PHA02884   137 MVTPIELA 144
PHA02741 PHA02741
hypothetical protein; Provisional
 454-506 8.38e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.49  E-value: 8.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1304473103  454 VTPFSR-----------DDRGQTPLHVAALCGQA----SLIDFLVSKGAVVNATD-YHGSTPLHLACQK 506
Cdd:PHA02741    40 FTPFIRgdchaaalnatDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEmLEGDTALHLAAHR 108
 
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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