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Conserved domains on  [gi|2462555837|ref|XP_054172374|]
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rabankyrin-5 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
640-702 5.70e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


:

Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 157.20  E-value: 5.70e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 640 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
177-515 1.08e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 177 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 256
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 257 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 336
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 337 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 416
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 417 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 496
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 2462555837 497 LLENGVDFAAVDENGNNAL 515
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-243 7.22e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 7.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  17 AAATQTHLTRRQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDV 96
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-------------------ETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  97 VSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSA 176
Cdd:COG0666   136 VKLLLEAGA-------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 177 LFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIA 243
Cdd:COG0666   203 KLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
Ank_2 pfam12796
Ankyrin repeats (3 copies);
482-561 5.03e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 482 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 561
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
 
Name Accession Description Interval E-value
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
640-702 5.70e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 157.20  E-value: 5.70e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 640 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
177-515 1.08e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 177 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 256
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 257 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 336
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 337 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 416
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 417 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 496
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 2462555837 497 LLENGVDFAAVDENGNNAL 515
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
641-702 1.49e-24

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 97.12  E-value: 1.49e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837  641 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:smart00064   2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-243 7.22e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 7.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  17 AAATQTHLTRRQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDV 96
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-------------------ETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  97 VSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSA 176
Cdd:COG0666   136 VKLLLEAGA-------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 177 LFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIA 243
Cdd:COG0666   203 KLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
PHA03095 PHA03095
ankyrin-like protein; Provisional
241-532 1.04e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.11  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 241 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWG 320
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 321 LEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSAEAILK 397
Cdd:PHA03095   95 TTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 398 R--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVN 472
Cdd:PHA03095  172 LliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISIN 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 473 ELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 532
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
641-703 2.49e-22

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 90.90  E-value: 2.49e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 641 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 703
Cdd:pfam01363   1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
Ank_2 pfam12796
Ankyrin repeats (3 copies);
414-508 6.36e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 6.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 414 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 493
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 2462555837 494 CSVLLENGVDFAAVD 508
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
265-383 4.46e-11

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: 66.19  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 339
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 340 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 383
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
482-561 5.03e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 482 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 561
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
PHA03100 PHA03100
ankyrin repeat protein; Provisional
439-617 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 439 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 513
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 514 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 576
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462555837 577 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 617
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
27-235 2.58e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  27 RQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAN 106
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG-------------------CYPIHIAIKHNFFDIIKLLLEKGAY 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 107 AlhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRqdSKSALFLLEHQADI 186
Cdd:PHA02874  183 A-------------NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIELLINNASI 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 187 NVSRTqDGETALQLAIrnQLPL---VVDAICTRGADMSVPDEKGNPPLWLAL 235
Cdd:PHA02874  248 NDQDI-DGSTPLHHAI--NPPCdidIIDILLYHKADISIKDNKGENPIDTAF 296
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-106 1.31e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  23 HLTRRQGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILE 102
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGHLEIVKLLLE 82

                  ....
gi 2462555837 103 QKAN 106
Cdd:pfam12796  83 KGAD 86
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
367-520 2.30e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 367 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 446
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 447 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 499
Cdd:TIGR00870 117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                         170       180
                  ....*....|....*....|.
gi 2462555837 500 NGVDFAAVDENGNNALHLAVM 520
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVM 217
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
308-337 2.50e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462555837  308 DGQTPLHLAASWGLEETVQCLLEFGANVNA 337
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
28-57 2.82e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.82e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462555837   28 QGETPLHTACRHGLANLTAELLQQGANPNL 57
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
640-702 5.70e-46

FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar proteins; ANFY1, also termed ankyrin repeats hooked to a zinc finger motif (Ankhzn), is a novel cytoplasmic protein that belongs to a new group of double zinc finger proteins involved in vesicle or protein transport. It is ubiquitously expressed in a spatiotemporal-specific manner and is located on endosomes. ANFY1 contains an N-terminal coiled-coil region and a BTB/POZ domain, ankyrin repeats in the middle, and a C-terminal FYVE domain.


Pssm-ID: 277267 [Multi-domain]  Cd Length: 63  Bit Score: 157.20  E-value: 5.70e-46
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 640 EPPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15728     1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
177-515 1.08e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 177 LFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcw 256
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 257 gpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVN 336
Cdd:COG0666    82 --AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR------------DKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 337 AQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHV 416
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP----------------------------------LHL 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 417 AVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSV 496
Cdd:COG0666   193 AAENGHLEIVKLLLEAGADVN--AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 2462555837 497 LLENGVDFAAVDENGNNAL 515
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-616 8.71e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 8.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 328 LLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVD 407
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 408 NKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQ 487
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVN--ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 488 QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHILGQYGKENAAAIFDLF 567
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2462555837 568 LEcmpgyPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQG 616
Cdd:COG0666   242 GA-----DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
107-413 6.99e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 6.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 107 ALHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADI 186
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 187 NVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWGPGpggcLQT 266
Cdd:COG0666    81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND----GNT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 267 LLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPI 346
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNAR------------DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 347 HVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNF 413
Cdd:COG0666   224 DLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-446 2.74e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 142 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRtQDGETALQLAIRNQLPLVVDAICTRGADMS 221
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALAD-ALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 222 VPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 301
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 302 geeeARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFA 381
Cdd:COG0666   150 ----DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALD 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 382 CAMTFKNNKSAEAILKREsGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKL 446
Cdd:COG0666   225 LAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
643-702 9.16e-25

FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) and similar proteins; Hrs, also termed protein pp110, is a tyrosine phosphorylated protein that plays an important role in the signaling pathway of HGF. It is localized to early endosomes and an essential component of the endosomal sorting and trafficking machinery. Hrs interacts with hypertonia-associated protein Trak1, a novel regulator of endosome-to-lysosome trafficking. It can also forms an Hrs/actinin-4/BERP/myosin V protein complex that is required for efficient transferrin receptor (TfR) recycling but not for epidermal growth factor receptor (EGFR) degradation. Moreover, Hrs, together with STAM proteins, STAM1 and STAM2, and EPs15, forms a multivalent ubiquitin-binding complex that sorts ubiquitinated proteins into the multivesicular body pathway, and plays a regulatory role in endocytosis/exocytosis. Furthermore, Hrs functions as an interactor of the neurofibromatosis 2 tumor suppressor protein schwannomin/merlin. It is also involved in the inhibition of citron kinase-mediated HIV-1 budding. Hrs contains a single ubiquitin-interacting motif (UIM) that is crucial for its function in receptor sorting, and a FYVE domain that harbors double Zn2+ binding sites.


Pssm-ID: 277260 [Multi-domain]  Cd Length: 61  Bit Score: 97.46  E-value: 9.16e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 643 WCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15720     2 WKDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL 61
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
641-702 1.49e-24

Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four proteins where it was first found: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn2+ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. The FYVE finger is structurally related to the PHD finger and the RING finger. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. The FYVE finger functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P), which is prominent on endosomes. The R+HHC+XCG motif is critical for PI3P binding.


Pssm-ID: 214499 [Multi-domain]  Cd Length: 68  Bit Score: 97.12  E-value: 1.49e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837  641 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:smart00064   2 PHWIPDEEvsnCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENL 66
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-243 7.22e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 7.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  17 AAATQTHLTRRQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDV 96
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG-------------------ETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  97 VSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSA 176
Cdd:COG0666   136 VKLLLEAGA-------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 177 LFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIA 243
Cdd:COG0666   203 KLLLEAGADVNA-KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
PHA03095 PHA03095
ankyrin-like protein; Provisional
241-532 1.04e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 105.11  E-value: 1.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 241 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEpTACFLIRSGCDVNSPrqpgangegeeeARDGQTPLHLAASWG 320
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD-IVRLLLEAGADVNAP------------ERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 321 LEETV-QCLLEFGANVNAQDAEGRTPIHVAISSQ--HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMtfKNNKSAEAILK 397
Cdd:PHA03095   95 TTLDViKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRK-GADVNALDLYGMTPLAVLL--KSRNANVELLR 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 398 R--ESGAAE-QVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVN 472
Cdd:PHA03095  172 LliDAGADVyAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISIN 251
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 473 ELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHgrlNNIRVLLT 532
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN---NNGRAVRA 308
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
641-703 2.49e-22

FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: Fab1, YOTB/ZK632.12, Vac1, and EEA1. The FYVE finger has been shown to bind two Zn++ ions. The FYVE finger has eight potential zinc coordinating cysteine positions. Many members of this family also include two histidines in a motif R+HHC+XCG, where + represents a charged residue and X any residue. We have included members which do not conserve these histidine residues but are clearly related.


Pssm-ID: 426221 [Multi-domain]  Cd Length: 68  Bit Score: 90.90  E-value: 2.49e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 641 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPII-KFDLNKPVRVCNICFDVLT 703
Cdd:pfam01363   1 PVWVPDSSatvCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-361 1.26e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  41 LANLTAELLQQGANPNLQTEEALPLPKEAASLTSLADSVHLQTPLHMAIAYNHPDVVSVILEQKANALHATNNLQIIPDF 120
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 121 SLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQL 200
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 201 AIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATcwgpgpggclqtllhrAIDENnepta 280
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN----------------AKDND----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 281 cflirsgcdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQL 360
Cdd:COG0666   219 ----------------------------GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                  .
gi 2462555837 361 L 361
Cdd:COG0666   271 L 271
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
649-699 2.01e-19

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 82.19  E-value: 2.01e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY 52
PHA02876 PHA02876
ankyrin repeat protein; Provisional
326-550 8.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 90.89  E-value: 8.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 326 QCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAaeq 405
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI--- 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 406 vdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGS-EIIVRNLLLAGAKVNELTKHRQTALHL 484
Cdd:PHA02876  238 --NKNDLSLLKAIRNEDLETSLLLYDAGFSVNS--IDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 485 AAQQDLPTI-CSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLH 550
Cdd:PHA02876  314 MAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIH 380
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
641-699 1.70e-18

FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 (spVps27p) and similar proteins; spVps27p, also termed suppressor of ste12 deletion protein 4 (Sst4p), is a conserved homolog of budding Saccharomyces cerevisiae Vps27 and of mammalian Hrs. It functions as a downstream factor for phosphatidylinositol 3-kinase (PtdIns 3-kinase) in forespore membrane formation with normal morphology. It colocalizes and interacts with Hse1p, a homolog of Saccharomyces cerevisiae Hse1p and of mammalian STAM, to form a complex whose ubiquitin-interacting motifs (UIMs) are important for sporulation. spVps27p contains a VHS (Vps27p/Hrs/Stam) domain, a FYVE domain, and two UIMs.


Pssm-ID: 277274 [Multi-domain]  Cd Length: 59  Bit Score: 79.50  E-value: 1.70e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 641 PPWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15735     1 PEWVDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY 59
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
392-622 1.82e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 392 AEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKV 471
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 472 NELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHI 551
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 552 LGQYGKEnaaAIFDLFLECmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGVNIFNY 622
Cdd:COG0666   160 AAANGNL---EIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
642-700 2.63e-18

FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; Lst2, also termed zinc finger FYVE domain-containing protein 28, is a monoubiquitinylated phosphoprotein that functions as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Unlike other FYVE domain-containing proteins, Lst2 displays primarily non-endosomal localization. Its endosomal localization is regulated by monoubiquitinylation. Lst2 physically binds Trim3, also known as BERP or RNF22, which is a coordinator of endosomal trafficking and interacts with Hrs and a complex that biases cargo recycling.


Pssm-ID: 277270 [Multi-domain]  Cd Length: 65  Bit Score: 79.31  E-value: 2.63e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 642 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFD 700
Cdd:cd15731     7 PDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCFM 65
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
641-702 4.61e-18

FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed endosome-associated protein p162, or zinc finger FYVE domain-containing protein 2, is an essential component of the endosomal fusion machinery and required for the fusion and maturation of early endosomes in endocytosis. It forms a parallel coiled-coil homodimer in cells. EEA1 serves as the p97 ATPase substrate and the p97 ATPase may regulate the size of early endosomes by governing the oligomeric state of EEA1. It can interact with the GTP-bound form of Rab22a and be involved in endosomal membrane trafficking. EEA1 also functions as an obligate scaffold for angiotensin II-induced Akt activation in early endosomes. It can be phosphorylated by p38 mitogen-activated protein kinase (MAPK) and further regulate mu opioid receptor endocytosis. EEA1 consists of an N-terminal C2H2 Zn2+ finger, four long heptad repeats, and a C-terminal region containing a calmodulin binding (IQ) motif, a Rab5 interaction site, and a FYVE domain. This model corresponds to the FYVE domain that is responsible for binding phosphatidyl inositol-3-phosphate (PtdIns3P or PI3P) on the membrane.


Pssm-ID: 277269 [Multi-domain]  Cd Length: 63  Bit Score: 78.59  E-value: 4.61e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 641 PPWCDGSY---CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 702
Cdd:cd15730     1 RKWADDEEvqnCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSSK--KPVRVCDACFDDL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-231 1.89e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.46  E-value: 1.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  27 RQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAn 106
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG-------------------NTPLHLAAANGNLEIVKLLLEAGA- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 107 alhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADI 186
Cdd:COG0666   178 ------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462555837 187 NVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPL 231
Cdd:COG0666   246 NA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
640-698 2.37e-17

FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ZF21 is phosphoinositide-binding protein that functions as a regulator of focal adhesions and cell movement through interaction with focal adhesion kinase. It can also bind to the cytoplasmic tail of membrane type 1 matrix metalloproteinase, a potent invasion-promoting protease, and play a key role in regulating multiple aspects of cancer cell migration and invasion. ZF21 contains a FYVE domain, which corresponds to this model.


Pssm-ID: 277266 [Multi-domain]  Cd Length: 64  Bit Score: 76.65  E-value: 2.37e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 640 EPPW---CDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNIC 698
Cdd:cd15727     1 EPPWvpdKECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNEC 62
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
646-702 2.40e-17

FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar proteins; WDFY3, also termed autophagy-linked FYVE protein (Alfy), is a ubiquitously expressed phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein required for selective macroautophagic degradation of aggregated proteins. It regulates the protein degradation through the direct interaction with the autophagy protein Atg5. Moreover, WDFY3 acts as a scaffold that bridges its cargo to the macroautophagic machinery via the creation of a greater complex with Atg12, Atg16L, and LC3. It also functionally associates with sequestosome-1/p62 (SQSTM1) in osteoclasts. WDFY3 shuttles between the nucleus and cytoplasm. It predominantly localizes to the nucleus and nuclear membrane under basal conditions, but is recruited to cytoplasmic ubiquitin-positive protein aggregates under stress conditions. WDFY3 contains a PH-BEACH domain assemblage, five WD40 repeats and a PtdIns3P-binding FYVE domain.


Pssm-ID: 277259 [Multi-domain]  Cd Length: 65  Bit Score: 76.66  E-value: 2.40e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 646 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15719     9 GDSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACYNIL 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
323-617 2.53e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 323 ETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNnksAEAILKR- 398
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEA-GADVNAPERCGFTPLHLYLYNAT---TLDVIKLl 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 399 -ESGA-AEQVDNKGRNFLHV--AVQNSDIESVLFLISVHANVNSRvqDASKLTPLH-LAVQAGSEI-IVRNLLLAGAKVN 472
Cdd:PHA03095  104 iKAGAdVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL--DLYGMTPLAvLLKSRNANVeLLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 473 ELTKHRQTALHLAAQ--QDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRvlltectvdaeafnlrgqsplh 550
Cdd:PHA03095  182 AVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL---------------------- 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 551 ilgqygkenaaaIFDLFLEcmpGYPLDKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 617
Cdd:PHA03095  240 ------------VLPLLIA---GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
PHA02874 PHA02874
ankyrin repeat protein; Provisional
186-544 6.66e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 6.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 186 INVSrTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCWgPGPggclq 265
Cdd:PHA02874   28 INIS-VDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL-PIP----- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 266 tllhraiDENNEpTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTP 345
Cdd:PHA02874  101 -------CIEKD-MIKTILDCGIDVNI------------KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 346 IHVAISSQHGVIIQLLVSHpDIHLNVRDRQGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNSDIES 425
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEK-GAYANVKDNNGESP----------------------------------LHNAAEYGDYAC 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 426 VLFLISVHANVNSRVQDAskLTPLHLAVQAGSEIIvrNLLLAGAKVNELTKHRQTALHLAAQQDLPT-ICSVLLENGVDF 504
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNG--FTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADI 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2462555837 505 AAVDENGNNALHLAVMH-GRLNNIRVLLTECTVDAEAFNLR 544
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLK 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
162-367 9.98e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 9.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 162 TLLHMAIQRQDSKSALFLLEHQADINVSRTQDgETAL-----QLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALA 236
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 237 NNLED--IASTLVRHGCDA---TCWGPGP------GGC-----LQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgang 300
Cdd:PHA03100  116 KKSNSysIVEYLLDNGANVnikNSDGENLlhlyleSNKidlkiLKLLIDKGVDINAKNRVNYLLSYGVPINIK------- 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 301 egeeearD--GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSH-PDI 367
Cdd:PHA03100  189 -------DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNgPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
311-555 1.05e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 311 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVshpdihLNVRDRQGLtPFACAmtfkNNK 390
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------DNGVDTSIL-PIPCI----EKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 391 SAEAILkrESGAAEQV-DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGA 469
Cdd:PHA02874  106 MIKTIL--DCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 470 KVNELTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRlNNIRVLLTECTVDAEAFNlrGQSP 548
Cdd:PHA02874  182 YANVKDNNGESPLHNAAEYgDYACI-KLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDID--GSTP 257

                  ....*..
gi 2462555837 549 LHILGQY 555
Cdd:PHA02874  258 LHHAINP 264
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
647-699 2.00e-16

FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also termed FYVE domain-containing dual specificity protein phosphatase 2 (FYVE-DSP2), or zinc finger FYVE domain-containing protein 11, is an dual specificity protein phosphatase that specifically dephosphorylates phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). It is localizes to early endosomes, as well as to Rab11- and Sec15-positive recycling endosomes, and regulates sorting from early endosomes. Moreover, MTMR4 is preferentially associated with and dephosphorylated the activated regulatory Smad proteins (R-Smads) in cytoplasm to keep transforming growth factor (TGF) beta signaling in homeostasis. It also functions as an essential negative modulator for the homeostasis of bone morphogenetic protein (BMP)/decapentaplegic (Dpp) signaling. In addition, MTMR4 acts as a novel interactor of the ubiquitin ligase Nedd4 (neural-precursor-cell-expressed developmentally down-regulated 4) and may play a role in the biological process of muscle breakdown. MTMR4 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain.


Pssm-ID: 277272 [Multi-domain]  Cd Length: 60  Bit Score: 74.00  E-value: 2.00e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 647 SYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15733     8 SHCFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
PHA02876 PHA02876
ankyrin repeat protein; Provisional
142-555 2.27e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.19  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 142 IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSrTQDGETALQLAIRNQLPLVVDAICtrgadms 221
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNII-ALDDLSVLECAVDSKNIDTIKAII------- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 222 vpDEKGNPplwlalanNLEDIAstlvrhgcdatcwgpgpggclqtlLHRAIDENNEPTACFLIRSGCDVNSPrqpgange 301
Cdd:PHA02876  232 --DNRSNI--------NKNDLS------------------------LLKAIRNEDLETSLLLYDAGFSVNSI-------- 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 302 geEEARDgqTPLHLAA-SWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV--IIQLLVSHPDIhlNVRDRQGLT 378
Cdd:PHA02876  270 --DDCKN--TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTenIRTLIMLGADV--NAADRLYIT 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 379 PFACAMTFKNNKsaeailkresgaaeqvdnkgrnflhvavqnsdiESVLFLISVHANVNSRvqDASKLTPLHLAVQAGSE 458
Cdd:PHA02876  344 PLHQASTLDRNK---------------------------------DIVITLLELGANVNAR--DYCDKTPIHYAAVRNNV 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 459 IIVRNLLLAGAKVNELTKHRQTALHLAAQQDLP-TICSVLLENGVDFAAVDENGNNALHLAVMHG-RLNNIRVLLtECTV 536
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLL-DNGA 467
                         410
                  ....*....|....*....
gi 2462555837 537 DAEAFNLRGQSPLHILGQY 555
Cdd:PHA02876  468 DVNAINIQNQYPLLIALEY 486
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
642-699 4.89e-16

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and similar proteins; scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif.


Pssm-ID: 277299 [Multi-domain]  Cd Length: 59  Bit Score: 72.71  E-value: 4.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 642 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKF-DLNKPVRVCNICF 699
Cdd:cd15760     1 HWKPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLgPLGVPQRVCDRCF 59
Ank_2 pfam12796
Ankyrin repeats (3 copies);
414-508 6.36e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 6.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 414 LHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRnLLLAGAKVNELTKHRqTALHLAAQQDLPTI 493
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDNGR-TALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 2462555837 494 CSVLLENGVDFAAVD 508
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
312-551 7.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.61  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 312 PLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVShpdihLNVRDRQGLTPFACAMTFKNNKS 391
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR-----SINKCSVFYTLVAIKDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 392 --AEAILKRESGAAEQVDNKgrnFLHVAVQNSDIES--VLFLISVHANVNSRVQDASKlTPLHLAVQAGSEIIVRNLLLA 467
Cdd:PHA02878  115 eiFKIILTNRYKNIQTIDLV---YIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 468 GAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVmhGRLNNIRVL--LTECTVDAEAFN-LR 544
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDILklLLEHGVDVNAKSyIL 268

                  ....*..
gi 2462555837 545 GQSPLHI 551
Cdd:PHA02878  269 GLTALHS 275
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
645-703 2.57e-14

FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This family includes a group of uncharacterized rab GTPase-binding effector proteins found in bilateria. Although their biological functions remain unclear, they all contain a FYVE domain that harbors a putative phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding site.


Pssm-ID: 277278 [Multi-domain]  Cd Length: 73  Bit Score: 68.14  E-value: 2.57e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 645 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiiKFDLNKPVRVCNICFDVLT 703
Cdd:cd15739     9 DVDQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVP--SGPNRRPARVCDVCHTLLV 65
Ank_2 pfam12796
Ankyrin repeats (3 copies);
313-439 4.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 4.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 313 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhlnvrdrqgltpfacamtfknnksa 392
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV------------------------- 55
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462555837 393 eailkresgaaeQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSR 439
Cdd:pfam12796  56 ------------NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
649-699 9.49e-14

FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, also termed FYVE finger-containing phosphoinositide kinase, or 1-phosphatidylinositol 3-phosphate 5-kinase, or phosphatidylinositol 3-phosphate 5-kinase (PIP5K3), or phosphatidylinositol 3-phosphate 5-kinase type III (PIPkin-III or type III PIP kinase), is a phosphoinositide 5-kinase that forms a complex with its regulators, the scaffolding protein Vac14 and the lipid phosphatase Fig4. The complex is responsible for synthesizing phosphatidylinositol 3,5-bisphosphate [PtdIns(3,5)P2] from phosphatidylinositol 3-phosphate (PtdIns3P or PI3P). Then phosphatidylinositol-5-phosphate (PtdIns5P) is generated directly from PtdIns(3,5)P2. PtdIns(3,5)P2 and PtdIns5P regulate endosomal trafficking and responses to extracellular stimuli. At this point, PIKfyve is vital in early embryonic development. Moreover, PIKfyve forms a complex with ArPIKfyve (associated regulator of PIKfyve) and SAC3 at the endomembranes, which plays a role in receptor tyrosine kinase (RTK) degradation. The phosphorylation of PIKfyve by AKT can facilitate Epidermal growth factor receptor (EGFR) degradation. In addition, PIKfyve may participate in the regulation of the glutamate transporters EAAT2, EAAT3 and EAAT4, and the cystic fibrosis transmembrane conductance regulator (CFTR). It is also essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle. It can be activated by protein kinase B (PKB/Akt) and further up-regulates human ether-a-go-go (hERG) channels. This family also includes the yeast and plant orthologs of human PIKfyve, Fab1. PIKfyve and its orthologs share a similar architecture. They contain an N-terminal FYVE domain, a middle region related to the CCT/TCP-1/Cpn60 chaperonins that are involved in productive folding of actin and tubulin, a second middle domain that contains a number of conserved cysteine residues (CCR) unique to this family, and a C-terminal lipid kinase domain related to PtdInsP kinases.


Pssm-ID: 277264 [Multi-domain]  Cd Length: 62  Bit Score: 66.19  E-value: 9.49e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15725    11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCC 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
449-531 1.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 449 LHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGvdFAAVDENGNNALHLAVMHGRLNNIR 528
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78

                  ...
gi 2462555837 529 VLL 531
Cdd:pfam12796  79 LLL 81
PHA03095 PHA03095
ankyrin-like protein; Provisional
114-398 1.35e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 114 LQIIPDFSLKDSRDQTVLGLALWTGMHT---IAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSAL-FLLEHQADINVs 189
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNA- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 190 RTQDGETALQLAIRNQL--PLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIA--STLVRHGCDATcwgpGPGGCLQ 265
Cdd:PHA03095  113 KDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVY----AVDDRFR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 266 TLLHRAIDENNEPTACF--LIRSGCDVNSPRqpgangegeeeaRDGQTPLHLAASWGLEET--VQCLLEFGANVNAQDAE 341
Cdd:PHA03095  189 SLLHHHLQSFKPRARIVreLIRAGCDPAATD------------MLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRY 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462555837 342 GRTPIHVA-ISSQHGVIIQLLVSHPDIhlNVRDRQGLTPFACAMTFKNNKSAEAILKR 398
Cdd:PHA03095  257 GQTPLHYAaVFNNPRACRRLIALGADI--NAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
649-699 1.46e-13

FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1 and RUFY2. RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions. Both RUFY1 and RUFY2 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277261 [Multi-domain]  Cd Length: 58  Bit Score: 65.48  E-value: 1.46e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFdlNKPVRVCNICF 699
Cdd:cd15721    10 CQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSS--AKPVRVCDTCY 58
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
641-699 1.88e-13

FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and similar proteins; This family includes WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2. WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. Both WDFY1 and WDFY2 contain a FYVE domain and multiple WD-40 repeats.


Pssm-ID: 277258 [Multi-domain]  Cd Length: 70  Bit Score: 65.81  E-value: 1.88e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 641 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLnkPVRVCNICF 699
Cdd:cd15718     1 PEWAESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRstIPVMGFEF--PVRVCNECY 70
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
645-702 2.64e-13

FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also termed FYVE-finger protein EIP1, or La-binding protein 1, or Rab4-interacting protein (Rabip4), or Zinc finger FYVE domain-containing protein 12 (ZFY12), a human homologue of mouse Rabip4, an effector of Rab4 GTPase that regulates recycling of endocytosed cargo. RUFY1 is an endosomal protein that functions as a dual effector of Rab4 and Rab14 and is involved in efficient recycling of transferrin (Tfn). It is a downstream effector of Etk, a downstream tyrosine kinase of PI3-kinase that is involved in regulation of vesicle trafficking. RUFY1 contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between.


Pssm-ID: 277297 [Multi-domain]  Cd Length: 71  Bit Score: 65.47  E-value: 2.64e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462555837 645 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 702
Cdd:cd15758    11 EATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYP--KPVRVCDSCHTLL 66
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
649-699 3.52e-13

FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also termed Myotubularin-related phosphatase 3, or FYVE domain-containing dual specificity protein phosphatase 1 (FYVE-DSP1), or zinc finger FYVE domain-containing protein 10, is a ubiquitously expressed phosphoinositide 3-phosphatase specific for phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and PIKfyve, which produces PtdIns(3,5)P2 from PtdIns3P. It regulates cell migration through modulating phosphatidylinositol 5-phosphate (PtdIns5P) levels. MTMR3 contains an N-terminal PH-GRAM (PH-G) domain, a MTM phosphatase domain, a coiled-coil region, and a C-terminal FYVE domain. Unlike conventional FYVE domains, the FYVE domain of MTMR3 neither confers endosomal localization nor binds to PtdIns3P. It is also not required for the enzyme activity of MTMR3. In contrast, the PH-G domain binds phosphoinositides.


Pssm-ID: 277271 [Multi-domain]  Cd Length: 61  Bit Score: 64.54  E-value: 3.52e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15732    11 CYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF 61
PHA02875 PHA02875
ankyrin repeat protein; Provisional
305-503 3.76e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 305 EARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACAM 384
Cdd:PHA02875   31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAT 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 385 TFKNNKSAEAILKResGAAEQVDNKGR-NFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRN 463
Cdd:PHA02875  111 ILKKLDIMKLLIAR--GADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKM 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462555837 464 LLLAGAKVNELTKHRQ-TALHLAAQQDLPTICSVLLENGVD 503
Cdd:PHA02875  187 LLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
125-427 4.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.92  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 125 SRDQTVLGL--ALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDgetalqlaI 202
Cdd:PHA02874   31 SVDETTTPLidAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPC--------I 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 203 RNQLplvVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCDATCwgPGPGGCLQtlLHRAIDENNEPTACF 282
Cdd:PHA02874  103 EKDM---IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI--EDDNGCYP--IHIAIKHNFFDIIKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 283 LIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIiQLLV 362
Cdd:PHA02874  176 LLEKGAYANV------------KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-ELLI 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 363 SHPDIhlNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVL 427
Cdd:PHA02874  243 NNASI--NDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVI 305
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-187 4.99e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 4.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  23 HLTRRQGETPLHTACRHGLANLTAELLQQGANPNLQTEealplpkeaasltsladsvHLQTPLHMAIAYNHPDVVSVILE 102
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-------------------DGETPLHLAAENGHLEIVKLLLE 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 103 QKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEH 182
Cdd:COG0666   208 AGA-------------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                  ....*
gi 2462555837 183 QADIN 187
Cdd:COG0666   275 LLLLA 279
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
649-702 5.74e-13

FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE domain-containing protein 16 (ZFY16), or endosome-associated FYVE domain protein, is a FYVE domain-containing protein that is localized to EEA1-containing endosomes. It is regulated by phosphoinositol lipid and engaged in endosome-mediated receptor modulation. Endofin is involved in Bone morphogenetic protein (BMP) signaling through interacting with Smad1 preferentially and enhancing Smad1 phosphorylation and nuclear localization upon BMP stimulation. It also functions as a scaffold protein that brings Smad4 to the proximity of the receptor complex in Transforming growth factor (TGF)-beta signaling. Moreover, endofin is a novel tyrosine phosphorylation target downstream of epidermal growth factor receptor (EGFR) in EGF-signaling. In addition, endofin plays a role in endosomal trafficking by recruiting cytosolic TOM1, an important molecule for membrane recruitment of clathrin, onto endosomal membranes.


Pssm-ID: 277268 [Multi-domain]  Cd Length: 68  Bit Score: 64.30  E-value: 5.74e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTkeipiIKFDL----NKPVRVCNICFDVL 702
Cdd:cd15729    16 CMQCEVKFTFTKRRHHCRACGKVLCSACCS-----LKARLeyldNKEARVCVPCYQTL 68
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
649-702 2.85e-12

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar proteins; Phafin-1, also termed lysosome-associated apoptosis-inducing protein containing PH (pleckstrin homology) and FYVE domains (LAPF), or pleckstrin homology domain-containing family F member 1 (PKHF1), or PH domain-containing family F member 1, or apoptosis-inducing protein, or PH and FYVE domain-containing protein 1, or zinc finger FYVE domain-containing protein 15, is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway.


Pssm-ID: 277293 [Multi-domain]  Cd Length: 64  Bit Score: 62.28  E-value: 2.85e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 649 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKE--IPIIKfdlNKPVRVCNICFDVL 702
Cdd:cd15754    11 CMRCTqTNFSLLTRRHHCRKCGFVVCHECSRQRflIPRLS---PKPVRVCSLCYRKL 64
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
649-699 3.25e-12

FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar proteins; ZFYV1, also termed double FYVE-containing protein 1 (DFCP1), or SR3, or tandem FYVE fingers-1, is a novel tandem FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. The subcellular distribution of exogenously-expressed ZFYV1 to Golgi, endoplasmic reticulum (ER) and vesicular is governed in part by its FYVE domains but unaffected by wortmannin, a PI3-kinase inhibitor. In addition to C-terminal tandem FYVE domain, ZFYV1 contains an N-terminal putative C2H2 type zinc finger and a possible nucleotide binding P-loop.


Pssm-ID: 277273 [Multi-domain]  Cd Length: 61  Bit Score: 61.96  E-value: 3.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15734    11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
76-504 3.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  76 ADSVHLQTPLHMAIAYNHPDVVSVILEQKAnalhatnnlqiipDFSLKDSRDQTVLGLALWT-GMHTIAAqLLGSGAAIN 154
Cdd:PHA02876  173 AKDIYCITPIHYAAERGNAKMVNLLLSYGA-------------DVNIIALDDLSVLECAVDSkNIDTIKA-IIDNRSNIN 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 155 dtmSDGQTLLHmAIQRQDSKSALFLLEHQADINvSRTQDGETALQLAIRN-QLPLVVDAICTRGADMSVPDEKGNPPLWL 233
Cdd:PHA02876  239 ---KNDLSLLK-AIRNEDLETSLLLYDAGFSVN-SIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 234 ALANnlediastlvrhgcdatcwgpgpggclqtllhrAIDENNEPTacfLIRSGCDVNSPRqpgangegeeeaRDGQTPL 313
Cdd:PHA02876  314 MAKN---------------------------------GYDTENIRT---LIMLGADVNAAD------------RLYITPL 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 314 HLAASWG-LEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpdihlnvrdrqgltpfacamtfknnksa 392
Cdd:PHA02876  346 HQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY---------------------------- 397
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 393 eailkreSGAAEQVDNKGRNFLHVAVQNSD-IESVLFLISVHANVNSRVQDASklTPLHLAVQAGSEI-IVRNLLLAGAK 470
Cdd:PHA02876  398 -------GADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS--TPLHYACKKNCKLdVIEMLLDNGAD 468
                         410       420       430
                  ....*....|....*....|....*....|....
gi 2462555837 471 VNELTKHRQTALHLAAQQDlpTICSVLLENGVDF 504
Cdd:PHA02876  469 VNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
649-699 4.21e-12

FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), and similar proteins; This family includes protein containing both PH and FYVE domains 1 (phafin-1) and 2 (phafin-2). Phafin-1 is a representative of a novel family of PH and FYVE domain-containing proteins called phafins. It is a ubiquitously expressed pro-apoptotic protein via translocating to lysosomes, facilitating apoptosis induction through a lysosomal-mitochondrial apoptotic pathway. Phafin-2 is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277257 [Multi-domain]  Cd Length: 61  Bit Score: 61.61  E-value: 4.21e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462555837 649 CYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKeipiiKFDL----NKPVRVCNICF 699
Cdd:cd15717    11 CMHCKkTKFTAINRRHHCRKCGAVVCGACSSK-----KFLLphqsSKPLRVCDTCY 61
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
642-699 4.25e-12

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar proteins; FGD6, also termed zinc finger FYVE domain-containing protein 24 is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) whose biological function remains unclear. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Moreover, the FYVE domain of FGD6 is a canonical FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site.


Pssm-ID: 277282 [Multi-domain]  Cd Length: 61  Bit Score: 61.68  E-value: 4.25e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462555837 642 PWCDGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 699
Cdd:cd15743     5 PDSRVTMCMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAPLEYLK-NKSARVCDECF 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
266-510 7.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 7.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 266 TLLHRAIDENNEPTACFLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLE-----ETVQCLLEFGANVNAQDA 340
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINS------------STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 341 EGRTPIHVAIS--SQHGVIIQLLVSHpdihlnvrdrqgltpfACAMTFKNNKsaeailkresgaaeqvdnkGRNFLHVAV 418
Cdd:PHA03100  105 NGITPLLYAISkkSNSYSIVEYLLDN----------------GANVNIKNSD-------------------GENLLHLYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 419 QNSDIES--VLFLISVHANVNSR--------------VQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTAL 482
Cdd:PHA03100  150 ESNKIDLkiLKLLIDKGVDINAKnrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
                         250       260
                  ....*....|....*....|....*...
gi 2462555837 483 HLAAQQDLPTICSVLLENGVDFAAVDEN 510
Cdd:PHA03100  230 HIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
405-572 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 405 QVDNKGRNFLH-----VAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQA--GSEIIVRNLLLAGAKVNELTKH 477
Cdd:PHA03100   63 SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN--APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 478 RQTALHLAAQQDLPT--ICSVLLENGVDFAA----------------VDENGNNALHLAVMHGRLNNIRVLLtECTVDAE 539
Cdd:PHA03100  141 GENLLHLYLESNKIDlkILKLLIDKGVDINAknrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPN 219
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462555837 540 AFNLRGQSPLH--ILGQYGkenaaAIFDLFLECMP 572
Cdd:PHA03100  220 LVNKYGDTPLHiaILNNNK-----EIFKLLLNNGP 249
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
642-702 1.74e-11

FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar proteins; Phafin-2, also termed endoplasmic reticulum-associated apoptosis-involved protein containing PH and FYVE domains (EAPF), or pleckstrin homology domain-containing family F member 2 (PKHF2), or PH domain-containing family F member 2, or PH and FYVE domain-containing protein 2, or zinc finger FYVE domain-containing protein 18, is a ubiquitously expressed endoplasmic reticulum-associated protein that facilitates tumor necrosis factor alpha (TNF-alpha)-triggered cellular apoptosis through endoplasmic reticulum (ER)-mitochondrial apoptotic pathway. It is an endosomal phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) effector, as well as an interactor of the endosomal-tethering protein EEA1. It regulates endosome fusion upstream of Rab5. Phafin-2 also functions as a novel regulator of endocytic epidermal growth factor receptor (EGFR) degradation through a role in endosomal fusion.


Pssm-ID: 277294 [Multi-domain]  Cd Length: 64  Bit Score: 60.05  E-value: 1.74e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 642 PWCDGSYCYECT-ARFGVTTRKHHCRHCGRLLCHKCSTKEIpIIKFDLNKPVRVCNICFDVL 702
Cdd:cd15755     4 PDSEATVCMRCQkAKFTPVNRRHHCRKCGFVVCGPCSEKKF-LLPSQSSKPVRVCDFCYDLL 64
PHA02878 PHA02878
ankyrin repeat protein; Provisional
84-364 1.77e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  84 PLHMAIAYNHPDVVSVILEQKANA----------LH----ATNNLQIIPDFSLKDSRDQTVLGLALWTGMHT----IAAQ 145
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVnqpdhrdltpLHiickEPNKLGMKEMIRSINKCSVFYTLVAIKDAFNNrnveIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 146 LLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDE 225
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 226 KGNPPLWLALANNLEDIASTLVRHGCDATCwgpgPGGCLQTLLHRAIDE-NNEPTACFLIRSGCDVNSprqpgangegeE 304
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDA----RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNA-----------K 264
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 305 EARDGQTPLHLAASwgLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV-IIQLLVSH 364
Cdd:PHA02878  265 SYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCInIGRILISN 323
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
641-702 3.11e-11

FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar proteins; WDFY1, also termed FYVE domain containing protein localized to endosomes-1 (FENS-1), or phosphoinositide-binding protein 1, or zinc finger FYVE domain-containing protein 17, is a novel single FYVE domain containing protein that binds phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) with high specificity over other phosphoinositides. WDFY1 to early endosomes requires an intact FYVE domain and is inhibited by wortmannin, a PI3-kinase inhibitor. In addition to FYVE domain, WDFY1 harbors multiple WD-40 repeats.


Pssm-ID: 277295 [Multi-domain]  Cd Length: 76  Bit Score: 59.70  E-value: 3.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 641 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNICFDVL 702
Cdd:cd15756     1 PQWLESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSKRssYPIMGFEFQ--VRVCDSCFETI 73
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
642-702 4.05e-11

FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and similar proteins; Rbsn-5, also termed zinc finger FYVE domain-containing protein 20, is a novel Rab5 effector that is complexed to the Sec1-like protein VPS45 and recruited in a phosphatidylinositol-3-kinase-dependent fashion to early endosomes. It also binds to Rab4 and EHD1/RME-1, two regulators of the recycling route, and is involved in cargo recycling to the plasma membrane. Moreover, Rbsn-5 regulates endocytosis at the apical side of the wing epithelium and plays a role of the apical endocytic trafficking of Fmi in the establishment of planar cell polarity (PCP).


Pssm-ID: 277256 [Multi-domain]  Cd Length: 61  Bit Score: 58.89  E-value: 4.05e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 642 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCHKCStkeipiiKFdLNKPVRVCNICFDVL 702
Cdd:cd15716     3 PWVNDSdvpFCPDCGKKFNLARRRHHCRLCGSIMCNKCS-------QF-LPLHIRCCHHCKDLL 58
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
265-383 4.46e-11

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: 66.19  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFGANVNAQD 339
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVSPR---ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 340 AEGRTPIHVAISSQHGV----IIQLLVSHpDIHLN------VRDRQGLTPFACA 383
Cdd:cd22192   167 SLGNTVLHILVLQPNKTfacqMYDLILSY-DKEDDlqpldlVPNNQGLTPFKLA 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
482-561 5.03e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 482 LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAeafNLRGQSPLHILGQYGKENAA 561
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
649-702 7.47e-11

FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia FGD1, FGD2, FGD4; This family represents a group of Rho GTPase cell division cycle 42 (Cdc42)-specific guanine nucleotide exchange factors (GEFs), including FYVE, RhoGEF and PH domain-containing protein FGD1, FGD2 and FGD4. FGD1, also termed faciogenital dysplasia 1 protein, or Rho/Rac guanine nucleotide exchange factor FGD1 (Rho/Rac GEF), or zinc finger FYVE domain-containing protein 3, is a central regulator of extracellular matrix remodeling and belongs to the DBL family of GEFs that regulate the activation of the Rho GTPases. FGD1 is encoded by gene FGD1. Disabling mutations in the FGD1 gene cause the human X-linked developmental disorder faciogenital dysplasia (FGDY, also known as Aarskog-Scott syndrome). FGD2, also termed zinc finger FYVE domain-containing protein 4, is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. It localizes to early endosomes and active membrane ruffles. It plays a role in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system. FGD4, also termed actin filament-binding protein frabin, or FGD1-related F-actin-binding protein, or zinc finger FYVE domain-containing protein 6, functions as an F-actin-binding (FAB) protein showing significant homology to FGD1. It induces the formation of filopodia through the activation of Cdc42 in fibroblasts. Those FGD proteins possess a similar domain organization that contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus. However, each FGD has a unique N-terminal region that may directly or indirectly interact with F-actin. FGD1 and FGD4 have an N-terminal proline-rich domain (PRD) and an N-terminal F-actin binding (FAB) domain, respectively. This model corresponds to the FYVE domain, which has been found in many proteins involved in membrane trafficking and phosphoinositide metabolism, and has been defined by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCR patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding site. FGD1 possesses a FYVE-like domain that lack the N-terminal WxxD motif. Moreover, FGD2 is the only known RhoGEF family member shown to have a functional FYVE domain and endosomal binding activity.


Pssm-ID: 277280 [Multi-domain]  Cd Length: 65  Bit Score: 58.27  E-value: 7.47e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 649 CYECTARF-GVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICFDVL 702
Cdd:cd15741    12 CMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAT-LEYDGNKLNRVCKHCYVIL 65
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
642-683 9.42e-11

FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the second FYVE domain that is responsible for the ability of Pep7p to efficiently interact with Vac1p and Vps45p.


Pssm-ID: 277276 [Multi-domain]  Cd Length: 83  Bit Score: 58.29  E-value: 9.42e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462555837 642 PWCDGS---YCYECTARFGVTTRKHHCRHCGRLLCH----KCSTkEIPI 683
Cdd:cd15737     1 PWEDDSsvtHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCST-EVPL 48
PHA02875 PHA02875
ankyrin repeat protein; Provisional
307-437 1.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 307 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIhLNVRDRQGLTPFACAMTF 386
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 387 KNNKSAEAILkrESGAaeQVDNKGRN----FLHVAVQNSDIESVLFLISVHANVN 437
Cdd:PHA02875  179 GDIAICKMLL--DSGA--NIDYFGKNgcvaALCYAIENNKIDIVRLFIKRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
308-370 2.11e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 2.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 308 DGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPDIHLN 370
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
31-361 2.54e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  31 TPLHTACRHGLANLTAELLQQGANPNLQTEEALplpkeaasltsladsvhlqTPLHMAIAYNHPDVVSVILEQKANA--- 107
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDL-------------------SVLECAVDSKNIDTIKAIIDNRSNInkn 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 108 ----LHATNNLQIIPDFSLKDSR---------DQTVLGLALWT-GMHTIAAQLLGSGAAINDTMSDGQTLLH-MAIQRQD 172
Cdd:PHA02876  241 dlslLKAIRNEDLETSLLLYDAGfsvnsiddcKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYD 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 173 SKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHGCD 252
Cdd:PHA02876  321 TENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 253 ATCWGPGPGgclqTLLHRAIDENNEPTAC-FLIRSGCDVNSprqpgangegeeEARDGQTPLHLAASWGLE-ETVQCLLE 330
Cdd:PHA02876  401 IEALSQKIG----TALHFALCGTNPYMSVkTLIDRGANVNS------------KNKDLSTPLHYACKKNCKlDVIEMLLD 464
                         330       340       350
                  ....*....|....*....|....*....|.
gi 2462555837 331 FGANVNAQDAEGRTPIHVAIsSQHGVIIQLL 361
Cdd:PHA02876  465 NGADVNAINIQNQYPLLIAL-EYHGIVNILL 494
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
647-700 2.86e-10

FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed FYVE domain-containing centrosomal protein (FYVE-CENT), or spastizin, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that localizes to the centrosome and midbody. ZFY26 and its interacting partners TTC19 and KIF13A are required for cytokinesis. It also interacts with Beclin 1, a subunit of class III phosphatidylinositol 3-kinase complex, and may have potential implications for carcinogenesis. In addition, it has been considered as the causal agent of a rare form of hereditary spastic paraplegia. ZFY26 contains a FYVE domain that is important for targeting of FYVE-CENT to the midbody.


Pssm-ID: 277263 [Multi-domain]  Cd Length: 61  Bit Score: 56.37  E-value: 2.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 647 SYCYECTA-RFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICFD 700
Cdd:cd15724     8 SVCMVCQVeRFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREN-PVRVCDQCYE 61
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
645-702 3.36e-10

FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also termed Rab4-interacting protein related, is a novel embryonic factor that contains an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between. It is present in the nucleus at early stages of embryonic development. It may have both endosomal functions in the cytoplasm and nuclear functions.


Pssm-ID: 277298 [Multi-domain]  Cd Length: 71  Bit Score: 56.57  E-value: 3.36e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462555837 645 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlnKPVRVCNICFDVL 702
Cdd:cd15759     9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLPSSP--KPVRVCDSCHAML 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
131-224 7.57e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 7.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 131 LGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHqadINVSRTQDGETALQLAIRNQLPLVV 210
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2462555837 211 DAICTRGADMSVPD 224
Cdd:pfam12796  78 KLLLEKGADINVKD 91
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
649-699 1.11e-09

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar proteins; FGD5, also termed zinc finger FYVE domain-containing protein 23, is an endothelial cell (EC)-specific guanine nucleotide exchange factor (GEF) that regulates endothelial adhesion, survival, and angiogenesis by modulating phosphatidylinositol 3-kinase signaling. It functions as a novel genetic regulator of vascular pruning by activation of endothelial cell-targeted apoptosis. FGD5 is a homologue of FGD1 and contains a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. The FYVE domain of FGD5 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277281 [Multi-domain]  Cd Length: 67  Bit Score: 54.94  E-value: 1.11e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPiIKFDLNKPVRVCNICF 699
Cdd:cd15742    12 CMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYP-LKYLKDRPAKVCDGCF 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
439-617 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 439 RVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQ-----DLPTICSVLLENGVDFAAVDENGNN 513
Cdd:PHA03100   29 DYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGIT 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 514 ALHLAVMHgRLNNIRV--LLTECTVDAEAFNLRGQSPLHILGQYGKE---------------NAAAIFDLFLECmpGYPL 576
Cdd:PHA03100  109 PLLYAISK-KSNSYSIveYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdiNAKNRVNYLLSY--GVPI 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2462555837 577 DKPDADGSTVLLLAYMKGNANLCRAIVRSGARLGVNNNQGV 617
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
649-699 1.71e-09

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 54.05  E-value: 1.71e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15745     2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
641-698 2.81e-09

FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also termed zinc finger FYVE domain-containing protein 22, or ProF (propeller-FYVE protein), is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding protein that is localized to a distinct subset of early endosomes close to the plasma membrane. It interacts preferentially with endogenous serine/threonine kinase Akt2, but not Akt1, and plays a specific role in modulating signaling through Akt downstream of the interaction of this kinase with the endosomal proteins APPL (adaptor protein containing PH domain, PTB domain, and leucine zipper motif). In addition to Akt, WDFY2 serves as a binding partner for protein kinase C, zeta (PRKCZ), and its substrate vesicle-associated membrane protein 2 (VAMP2), and is involved in vesicle cycling in various secretory pathways. Moreover, Silencing of WDFY2 by siRNA produces a strong inhibition of endocytosis. WDFY2 contains WD40 motifs and a FYVE domain.


Pssm-ID: 277296 [Multi-domain]  Cd Length: 70  Bit Score: 53.92  E-value: 2.81e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 641 PPWCDGSYCYECTARF-----------GVTTRKHHCRHCGRLLCHKCSTKE--IPIIKFDLNkpVRVCNIC 698
Cdd:cd15757     1 PEWLDSDSCQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSKRstIPLMGFEFE--VRVCDSC 69
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
649-699 4.87e-09

FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ZFY19, also termed mixed lineage leukemia (MLL) partner containing FYVE domain, is encoded by a novel gene, MLL partner containing FYVE domain (MPFYVE). The FYVE domain of ZFY19 resembles FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. The biological function of ZFY19 remains unclear.


Pssm-ID: 277288 [Multi-domain]  Cd Length: 51  Bit Score: 52.51  E-value: 4.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDlNKPVRVCNICF 699
Cdd:cd15749     2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKG-NQKQKVCKQCH 51
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
309-436 1.41e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 309 GQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLL-----VSHPDIHLNVrdrqgltpfACA 383
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasISDPHAAGDL---------LCT 628
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 384 MTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANV 436
Cdd:PLN03192  629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
311-362 1.64e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.64e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 311 TPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLV 362
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
198-292 2.09e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 198 LQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRHgCDATCWGPGpggclQTLLHRAIDENNE 277
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-----RTALHYAARSGHL 74
                          90
                  ....*....|....*
gi 2462555837 278 PTACFLIRSGCDVNS 292
Cdd:pfam12796  75 EIVKLLLEKGADINV 89
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
649-699 3.11e-08

FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; The family includes Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 (scVps27p) and protein VAC1 (Vac1p). scVps27p, also termed Golgi retention defective protein 11, is the putative yeast counterpart of the mammalian protein Hrs and is involved in endosome maturation. It is a mono-ubiquitin-binding protein that interacts with ubiquitinated cargoes, such as Hse1p, and is required for protein sorting into the multivesicular body. Vps27p forms a complex with Hse1p. The complex binds ubiquitin and mediates endosomal protein sorting. At the endosome, Vps27p and a trimeric protein complex, ESCRT-1, bind ubiquitin and are important for multivesicular body (MVB) sorting. Vps27p contains an N-terminal VHS (Vps27/Hrs/STAM) domain, a FYVE domain that binds PtdIns3P, followed by two ubiquitin-interacting motifs (UIMs), and a C-terminal clathrin-binding motif. Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The FYVE domain in both Vps27p and Vac1p harbors a zinc-binding site composed of seven Cysteines and one Histidine, which is different from that of other FYVE domain containing proteins.


Pssm-ID: 277275 [Multi-domain]  Cd Length: 56  Bit Score: 50.64  E-value: 3.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPI---IKFDLN-KPVRVCNICF 699
Cdd:cd15736     2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLnlsAYDPRNgKWYRCCHSCF 56
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
651-699 3.50e-08

FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from eumetazoa; This family includes a group of uncharacterized myotubularin-related proteins mainly found in eumetazoa. Although their biological functions remain unclear, they share similar domain architecture that consists of an N-terminal pleckstrin homology (PH) domain, a highly conserved region related to myotubularin proteins, a C-terminal FYVE domain. The model corresponds to the FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277277 [Multi-domain]  Cd Length: 61  Bit Score: 50.40  E-value: 3.50e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462555837 651 ECTARFGVTTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15738    13 SCSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY 61
PHA02878 PHA02878
ankyrin repeat protein; Provisional
264-466 5.12e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 264 LQTLLHRAIDENNEPTACFLIRSGCDVNSPRqpgangegeeeaRDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGR 343
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPD------------KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 344 TPIHVAISSQHGV-IIQLLVSHpDIHLNVRDR-QGLTPfacamtfknnksaeailkresgaaeqvdnkgrnfLHVAVQNS 421
Cdd:PHA02878  236 TPLHISVGYCKDYdILKLLLEH-GVDVNAKSYiLGLTA----------------------------------LHSSIKSE 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462555837 422 DIESVLflISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL 466
Cdd:PHA02878  281 RKLKLL--LEYGADINS--LNSYKLTPLSSAVKQYLCINIGRILI 321
Ank_2 pfam12796
Ankyrin repeats (3 copies);
268-339 5.17e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 5.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 268 LHRAIDENNEPTACFLIRSGCDVNSPRQPG-------ANGEGEEEAR------------DGQTPLHLAASWGLEETVQCL 328
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGrtalhlaAKNGHLEIVKlllehadvnlkdNGRTALHYAARSGHLEIVKLL 80
                          90
                  ....*....|.
gi 2462555837 329 LEFGANVNAQD 339
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
414-607 8.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 8.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 414 LHVAVQNSDIESVLFLISVHANVNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELT-KHRQTALHLAAQQDLPT 492
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE--SELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 493 ICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtectvdaeafnlrgqsplhilgqygKENAAaifdlflecmp 572
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI-------------------------DHKAC----------- 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462555837 573 gypLDKPDADGSTVLLLAYMKGNANLCRAIVRSGA 607
Cdd:PHA02875  161 ---LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
645-699 1.20e-07

FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar proteins; FYCO1, also termed zinc finger FYVE domain-containing protein 7, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that is associated with the exterior of autophagosomes and mediates microtubule plus-end-directed vesicle transport. It acts as an effector of GTP-bound Rab7, a GTPase that recruits FYCO1 to autophagosomes and has been implicated in autophagosome-lysosomal fusion. FYCO1 also interacts with two microtubule motor proteins, kinesin (KIF) 5B and KIF23, and thus functions as a platform for assembly of vesicle fusion and trafficking factors. FYCO1 contains an N-terminal alpha-helical RUN domain followed by a long central coiled-coil region, a FYVE domain and a GOLD (Golgi dynamics) domain in C-terminus.


Pssm-ID: 277265 [Multi-domain]  Cd Length: 58  Bit Score: 48.71  E-value: 1.20e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 645 DGSYCYECTARFGVTTRKHHCRHCGRLLCHKCStkEIPIIKFDLNKPVRVCNICF 699
Cdd:cd15726     6 DVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACS--NFYVLTAHGGKKERCCKACF 58
PHA02874 PHA02874
ankyrin repeat protein; Provisional
27-235 2.58e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  27 RQGETPLHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEQKAN 106
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG-------------------CYPIHIAIKHNFFDIIKLLLEKGAY 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 107 AlhatnnlqiipdfSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRqdSKSALFLLEHQADI 186
Cdd:PHA02874  183 A-------------NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIELLINNASI 247
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 187 NVSRTqDGETALQLAIrnQLPL---VVDAICTRGADMSVPDEKGNPPLWLAL 235
Cdd:PHA02874  248 NDQDI-DGSTPLHHAI--NPPCdidIIDILLYHKADISIKDNKGENPIDTAF 296
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
101-249 3.68e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 101 LEQKANALHATNNLQIIPDFSL--KDSRDQTVLglalwtgmHTIAA---QLLGSGaaindtmsdgqtllhmaiqrqDSKS 175
Cdd:PTZ00322   47 IDTHLEALEATENKDATPDHNLttEEVIDPVVA--------HMLTVelcQLAASG---------------------DAVG 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 176 ALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTLVRH 249
Cdd:PTZ00322   98 ARILLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
29-213 3.98e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  29 GETPLHTACRHGLANLTAELLQQGANPNLQTEealplpkeaasltsladsvHLQTPLHMAIAYNHPDVVSVILEQkanal 108
Cdd:PHA02874  157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN-------------------NGESPLHNAAEYGDYACIKLLIDH----- 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 109 haTNNLqiipdfSLKDSRDQTVLGLALwtgMHTIAA-QLLGSGAAINDTMSDGQTLLHMAIQRQDSKSAL-FLLEHQADI 186
Cdd:PHA02874  213 --GNHI------MNKCKNGFTPLHNAI---IHNRSAiELLINNASINDQDIDGSTPLHHAINPPCDIDIIdILLYHKADI 281
                         170       180
                  ....*....|....*....|....*....
gi 2462555837 187 NVsRTQDGETALQLAIR--NQLPLVVDAI 213
Cdd:PHA02874  282 SI-KDNKGENPIDTAFKyiNKDPVIKDII 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
32-252 9.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.89  E-value: 9.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  32 PLHTACRHGLANLTAELLQQGANPNLqteeaLPLPK-EAASLTSLADS--------VHLQTPLHMAIAYNHPDVVSVILE 102
Cdd:PHA02874   71 PLLTAIKIGAHDIIKLLIDNGVDTSI-----LPIPCiEKDMIKTILDCgidvnikdAELKTFLHYAIKKGDLESIKMLFE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 103 QKAnalhatnnlqiipDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEH 182
Cdd:PHA02874  146 YGA-------------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH 212
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 183 QADINVsRTQDGETALQLAI---RNQLPLVVDaictrGADMSVPDEKGNPPLWLALANNLE-DIASTLVRHGCD 252
Cdd:PHA02874  213 GNHIMN-KCKNGFTPLHNAIihnRSAIELLIN-----NASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKAD 280
PHA02874 PHA02874
ankyrin repeat protein; Provisional
417-556 1.07e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 417 AVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQAGSEIIVRNLLL-----------------------AGAKVNE 473
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINH--INTKIPHPLLTAIKIGAHDIIKLLIDngvdtsilpipciekdmiktildCGIDVNI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 474 LTKHRQTALHLAAQQ-DLPTIcSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPLHIL 552
Cdd:PHA02874  120 KDAELKTFLHYAIKKgDLESI-KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNA 197

                  ....
gi 2462555837 553 GQYG 556
Cdd:PHA02874  198 AEYG 201
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
265-454 1.17e-06

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: 51.72  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVNSPR-----QPGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFG---ANVN 336
Cdd:cd22193    77 QTALHIAIERRQGDIVALLVENGADVHAHAkgrffQPKYQGEG---FYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 337 AQDAEGRTPIH--VAIS-----------SQHGVIIQLLVS-HPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRE-- 399
Cdd:cd22193   154 AQDSRGNTVLHalVTVAdntkentkfvtRMYDMILIRGAKlCPTVELEeIRNNDGLTPLQLAAKMGKIEILKYILQREik 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 400 SGAAEQVDNKGRNFLHVAVQNS--DI--------ESVLFLISVHANVNSRvQDASKLTPLHLAVQ 454
Cdd:cd22193   234 EPELRHLSRKFTDWAYGPVSSSlyDLsnvdtcekNSVLEIIVYNSKIDNR-HEMLTLEPLNTLLQ 297
PHA02946 PHA02946
ankyin-like protein; Provisional
320-552 1.30e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.59  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 320 GLEET-VQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHpdihlnvrdrqGLTPFACAmtfKNNKSAEAILkr 398
Cdd:PHA02946   49 GLDERfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTH-----------GADPNACD---KQHKTPLYYL-- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 399 eSGAAEQVdnkgrnflhvavqnsdIESVLFLISVHANVNSRVqDASKLTPLhLAVQAGSEIIVRNLLLAGAKVNELTKHR 478
Cdd:PHA02946  113 -SGTDDEV----------------IERINLLVQYGAKINNSV-DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFG 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462555837 479 QTALHLAAQQDLPTICSV--LLENGVDFAAVDENGNNALHLaVMHGRLNNIRVL-LTECTVDAEAFNLRGQSPLHIL 552
Cdd:PHA02946  174 KNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI-VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLL 249
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
265-454 1.37e-06

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: 51.80  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVnsprQPGANGEGEEEARD-----GQTPLHLAASWGLEETVQCLLEFG---ANVN 336
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADV----SARATGRFFRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALE 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 337 AQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESG 401
Cdd:cd21882   150 AQDSLGNTVLHAlvlqadntpensafVCQMYNLLLSYGAHLDPTQQLEeIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462555837 402 AAEQvdNKGRNF-------LHVA------VQNSDIESVLFLISVHANVNSRvQDASKLTPLHLAVQ 454
Cdd:cd21882   230 GPYQ--PLSRKFtewtygpVTSSlydlseIDSWEKNSVLELIAFSKKREAR-HQMLVQEPLNELLQ 292
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
450-540 1.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 450 HLAVqAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRV 529
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|.
gi 2462555837 530 LLTECTVDAEA 540
Cdd:PTZ00322  167 LSRHSQCHFEL 177
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
649-699 1.75e-06

FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar proteins; FGD3, also termed zinc finger FYVE domain-containing protein 5, is a putative Cdc42-specific guanine nucleotide exchange factor (GEF) that undergoes the ubiquitin ligase SCFFWD1/beta-TrCP-mediated proteasomal degradation. It is a homologue of FGD1 and contains a DBL homology (DH) domain and pleckstrin homology (PH) domain in the middle region, a FYVE domain, and another PH domain in the C-terminus, but lacks the N-terminal proline-rich domain (PRD) found in FGD1. Due to this difference, FGD3 may play different roles from that of FGD1 to regulate cell morphology or motility. The FYVE domain of FGD3 resembles a FYVE-like domain that is different from the canonical FYVE domains, since it lacks one of the three conserved signature motifs (the WxxD motif) that are involved in phosphatidylinositol 3-phosphate (PtdIns3P or PI3P) binding and exhibits altered lipid binding specificities.


Pssm-ID: 277279 [Multi-domain]  Cd Length: 54  Bit Score: 45.38  E-value: 1.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 649 CYECTARFG-VTTRKHHCRHCGRLLCHKCSTkeipiIKFDLNKPVRVCNICF 699
Cdd:cd15740     8 CKGCNESFNsITKRRHHCKQCGAVICGKCSE-----FKDLASRHNRVCRDCF 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
480-531 1.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 480 TALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLL 531
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
82-220 2.64e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  82 QTPLHMAIAYNHPDVVSVILEqkanalHATNnlqiipdFSLKDSRDQTVLGLALWTGMHTIaAQLLGSGAAINDTMSDGQ 161
Cdd:PLN03192  559 RTPLHIAASKGYEDCVLVLLK------HACN-------VHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHAAGD 624
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 162 tLLHMAIQRQDSKSALFLLEHQADINvSRTQDGETALQLAIRNQLPLVVDAICTRGADM 220
Cdd:PLN03192  625 -LLCTAAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02946 PHA02946
ankyin-like protein; Provisional
304-484 4.63e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 4.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 304 EEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVI--IQLLVSHPDIHLNVRDRQGLTP-F 380
Cdd:PHA02946   67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSVDEEGCGPlL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 381 ACamtfknNKSAEAILKRESG---AAEQVDNKGRNFLHVAVQNSDIESVLFLISVHANVNSRVQDASKLTPLHLAV-QAG 456
Cdd:PHA02946  147 AC------TDPSERVFKKIMSigfEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCsKTV 220
                         170       180
                  ....*....|....*....|....*...
gi 2462555837 457 SEIIVRNLLLAGAKVNELTKHRQTALHL 484
Cdd:PHA02946  221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
308-339 5.22e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 5.22e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462555837 308 DGQTPLHLAA-SWGLEETVQCLLEFGANVNAQD 339
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
296-501 5.94e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 296 PGANGeGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQ 375
Cdd:PLN03192  513 LGDNG-GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDAN 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 376 GLTPFACAMTFKNNKSAEaILKRESGAAEQvdNKGRNFLHVAVQNSDIESVLFLISVHANVNSrvQDASKLTPLHLAVQA 455
Cdd:PLN03192  591 GNTALWNAISAKHHKIFR-ILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDS--EDHQGATALQVAMAE 665
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 456 GSEIIVRNLLLAGAKV--------------NELTKHRQTALHLAAQQDLPTICSVLLENG 501
Cdd:PLN03192  666 DHVDMVRLLIMNGADVdkantdddfsptelRELLQKRELGHSITIVDSVPADEPDLGRDG 725
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
265-450 8.25e-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: 48.99  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVNSPRQ-----PGANGEGeeeARDGQTPLHLAASWGLEETVQCLLEFGA-NVNAQ 338
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnPKYKHEG---FYFGETPLALAACTNQPEIVQLLMEKEStDITSQ 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 339 DAEGRTPIHVAIS------SQHGVIIQL----LVSHPDIHLN-VRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQVd 407
Cdd:cd22194   219 DSRGNTVLHALVTvaedskTQNDFVKRMydmiLLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSREIKEKPNR- 297
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462555837 408 NKGRNFLHVA---VQNS--DI--------ESVLFLISVHANVNSRvQDASKLTPLH 450
Cdd:cd22194   298 SLSRKFTDWAygpVSSSlyDLtnvdtttdNSVLEIIVYNTNIDNR-HEMLTLEPLH 352
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
662-699 9.14e-06

FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also termed Rap2-interacting protein x (RIPx or RPIPx), or single axon-regulated protein (singar), is an N-terminal RUN domain and a C-terminal FYVE domain containing protein predominantly expressed in the brain. It suppresses formation of surplus axons for neuronal polarity. Unlike other RUFY proteins, RUFY3 can associate with the GTP-bound active form of Rab5. Moreover, the FYVE domain of RUFY3 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue).


Pssm-ID: 277283 [Multi-domain]  Cd Length: 52  Bit Score: 43.18  E-value: 9.14e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462555837 662 KHHCRHCGRLLCHKCSTKEIPIIKFDLNkPVRVCNICF 699
Cdd:cd15744    16 KHNCYNCGGTFCDACSSNELPLPSSIYE-PARVCDVCY 52
PHA02741 PHA02741
hypothetical protein; Provisional
309-390 9.60e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 46.57  E-value: 9.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 309 GQTPLHLAA----SWGLEETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFACA 383
Cdd:PHA02741   60 GQMCIHIAAekheAQLAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139

                  ....*..
gi 2462555837 384 MTFKNNK 390
Cdd:PHA02741  140 IDNEDVA 146
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
649-702 9.99e-06

FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc finger FYVE domain-containing protein 27 (ZFY27 or ZFYVE27), is a FYVE domain-containing protein involved in transport of neuronal cargoes and implicated in the onset of hereditary spastic paraplegia (HSP). It is involved in neurite outgrowth through binding to spastin. Moreover, it functions as a key regulator of the Rab11-dependent membrane trafficking during neurite extension. It serves as an adaptor molecule that links its associated proteins, such as Rab11-GDP, VAP-A and -B, Surf4, and RTN3, to KIF5, a motor protein that mediates anterograde vesicular transport in neurons, and thus plays a key role in the maintenance of neuronal function. The FYVE domain of protrudin resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. In addition, unlike canonical FYVE domains that is located to early endosomes and specifically binds to phosphatidylinositol 3-phosphate (PtdIns3P or PI3P), the FYVE domain of protrudin is located to plasma membrane and preferentially binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). In addition to FYVE-related domain, protrudin also contains a Rab11-binding domain (RBD11), two hydrophobic domains, HP-1 and HP-2, an FFAT motif, and a coiled-coil domain.


Pssm-ID: 277262 [Multi-domain]  Cd Length: 62  Bit Score: 43.64  E-value: 9.99e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 649 CYECTARFGV-TTRKHHCRHCGRLLCHKCSTKEIPIIKFDLNKP------VRVCNICFDVL 702
Cdd:cd15723     2 CTGCGASFSVlLKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPaaqretVFVCSGCNDKL 62
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
265-465 1.08e-05

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: 48.99  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRA---IDENNEPTACFLIrSGCDVNSPRQPGANGEGEEEARDGQTPLHLAASWGLEETVQCLLEFGANVNAQdae 341
Cdd:cd22194    95 KTCLMKAllnINENTKEIVRILL-AFAEENGILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAH--- 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 342 grtpihvaissQHGVIIQLLVSHPDIHLnvrdrqGLTPFACAMTFKNNKSAEAILKRESGAAEQVDNKGRNFLHVAVQNS 421
Cdd:cd22194   171 -----------AKGVFFNPKYKHEGFYF------GETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTVA 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 422 D---------IESVLFLISVHANVN-SRVQDASKLTPLHLAVQAGSEIIVRNLL 465
Cdd:cd22194   234 EdsktqndfvKRMYDMILLKSENKNlETIRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-106 1.31e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  23 HLTRRQGETPLHTACRHGLANLTAELLQQgANPNLQTEEalplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILE 102
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--------------------RTALHYAARSGHLEIVKLLLE 82

                  ....
gi 2462555837 103 QKAN 106
Cdd:pfam12796  83 KGAD 86
PHA02859 PHA02859
ankyrin repeat protein; Provisional
419-551 1.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 419 QNSDIESVLFLISVHANVNSRVQDaSKLTPLH--LAVQAGSEI-IVRNLLLAGAKVNELTKHRQTALHLAAqqdlpTICS 495
Cdd:PHA02859   62 DKVNVEILKFLIENGADVNFKTRD-NNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMYM-----CNFN 135
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 496 V-------LLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLTECTVDAEAFNLRGQSPLHI 551
Cdd:PHA02859  136 VrinviklLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
FYVE1_Vac1p_like cd15761
FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also ...
646-699 1.65e-05

FYVE-related domain 1 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed vacuolar segregation protein Pep7p, or carboxypeptidase Y-deficient protein 7, or vacuolar protein sorting-associated protein 19 (Vps19p), or vacuolar protein-targeting protein 19, is a phosphatidylinositol 3-phosphate (PtdIns3P or PI3P)-binding protein that interacts with a Rab GTPase, GTP-bound form of Vps21p, and a Sec1p homologue, Vps45p, to facilitate Vps45p-dependent vesicle-mediated vacuolar protein sorting. It also acts as a novel regulator of vesicle docking and/or fusion at the endosome and functions in vesicle-mediated transport of Golgi precursor carboxypeptidase Y (CPY), protease A (PrA), protease B (PrB), but not alkaline phosphatase (ALP) from the trans-Golgi network-like compartment (TGN) to the endosome. Vac1p contains an N-terminal classical TFIIIA-like zinc finger, two putative zinc-binding FYVE fingers, and a C-terminal coiled coil region. The family corresponds to the first FYVE domain, which resembles the FYVE-related domain as it has an altered sequence in the basic ligand binding patch.


Pssm-ID: 277300  Cd Length: 76  Bit Score: 43.41  E-value: 1.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 646 GSYCYECTARFGVTTRKHHCRHCGRLLCHKCSTKeipIIKFDLNKPV--------RVCNICF 699
Cdd:cd15761    10 KSRCSECGKTLNKKNGIVNCRKCGELFCNEHCRN---RIKLNNSAEYdpkngkwcRCCEKCF 68
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
367-520 2.30e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 367 IHLNVRDRQGLTPFACAMTFKNNKSAEAILKRESGAAEQvdnkGRNFLHVAVQNsdIESVLFLISVHANVNSRVQDASKL 446
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLE--YVDAVEAILLHLLAAFRKSGPLEL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 447 -------------TPLHLAVQAGSEIIVRNLLLAGAKV------NELTK--------HRQTALHLAAQQDLPTICSVLLE 499
Cdd:TIGR00870 117 andqytseftpgiTALHLAAHRQNYEIVKLLLERGASVparacgDFFVKsqgvdsfyHGESPLNAAACLGSPSIVALLSE 196
                         170       180
                  ....*....|....*....|.
gi 2462555837 500 NGVDFAAVDENGNNALHLAVM 520
Cdd:TIGR00870 197 DPADILTADSLGNTLLHLLVM 217
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
410-595 2.38e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.70  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 410 GRNFLHVAVQNSDIESVLFLI-SVHANVNSRVqdASKL----TPLHLAVQAGSEIIVRNLLLAGAKVNeltKHRQTA--- 481
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMeAAPELVNEPM--TSDLyqgeTALHIAVVNQNLNLVRELIARGADVV---SPRATGtff 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 482 --------------LHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMhgrlnnirvlltectvdaeafnlrgqs 547
Cdd:cd22192   126 rpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL--------------------------- 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462555837 548 plhilgQYGKENAAAIFDLFLECMPG---YPLDK-PDADGSTVLLLAYMKGN 595
Cdd:cd22192   179 ------QPNKTFACQMYDLILSYDKEddlQPLDLvPNNQGLTPFKLAAKEGN 224
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
308-337 2.50e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.50e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462555837  308 DGQTPLHLAASWGLEETVQCLLEFGANVNA 337
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
88-336 3.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  88 AIAYNHPDVVSVILeqkanalhatnNLQIIPDFSLKDSRDQTVLGLALwtgMHTIAAQLLGSGAAINDTMSDG-QTLLHM 166
Cdd:PHA02875    9 AILFGELDIARRLL-----------DIGINPNFEIYDGISPIKLAMKF---RDSEAIKLLMKHGAIPDVKYPDiESELHD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 167 AIQRQDSKSALFLLEHQADINVSRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDEKGNPPLWLALANNLEDIASTL 246
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 247 VRHgcdatcwgpgpggclqtllhraidennepTACFLIRSGCdvnsprqpgangegeeeardGQTPLHLAASWGLEETVQ 326
Cdd:PHA02875  155 IDH-----------------------------KACLDIEDCC--------------------GCTPLIIAMAKGDIAICK 185
                         250
                  ....*....|
gi 2462555837 327 CLLEFGANVN 336
Cdd:PHA02875  186 MLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
33-156 3.92e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 3.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  33 LHTACRHGLANLTAELLQQGANPNLQTEEAlplpkeaasltsladsvhlQTPLHMAIAYNHPDVVSVILEqkanalHATN 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNG-------------------RTALHLAAKNGHLEIVKLLLE------HADV 55
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462555837 113 NLQiipdfslkdSRDQTVLGLALWTGMHTIAAQLLGSGAAINDT 156
Cdd:pfam12796  56 NLK---------DNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
27-188 8.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  27 RQGETPLHTACRHGLANLT--AELLQQGANPNLQTEEALPLpkeaasltsladsvhlqtpLHMAIAYNHPD--VVSVILE 102
Cdd:PHA03100  104 NNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENL-------------------LHLYLESNKIDlkILKLLID 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 103 QKANaLHATNNLQII----PDFSLKDSRDQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALF 178
Cdd:PHA03100  165 KGVD-INAKNRVNYLlsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|
gi 2462555837 179 LLEHQADINV 188
Cdd:PHA03100  244 LLNNGPSIKT 253
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
649-698 8.23e-05

FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 are a novel group of caspase regulators by the presence of a FYVE-type zinc finger domain. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD (x for any residue) motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains.


Pssm-ID: 277289 [Multi-domain]  Cd Length: 47  Bit Score: 40.42  E-value: 8.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462555837 649 CYECTARFGVTTRKHHCRHCGRLLCHKCSTKEipiikfdlNKPVRVCNIC 698
Cdd:cd15750     3 CESCGAKFSVFKRKRTCADCKRYFCSNCLSKE--------ERGRRRCRRC 44
PHA02878 PHA02878
ankyrin repeat protein; Provisional
25-251 8.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  25 TRRQGETPLHTACRHGLANLTAELLQQGANPNlqteealpLPKEAAsltsladsvhlQTPLHMAIAYNHPDVVSVILEqk 104
Cdd:PHA02878  164 DRHKGNTALHYATENKDQRLTELLLSYGANVN--------IPDKTN-----------NSPLHHAVKHYNKPIVHILLE-- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 105 analhatnnlqiipdfslkdsrdqtvlglalwtgmhtiaaqllgSGAAINDTMSDGQTLLHMAIQRQDSKSAL-FLLEHQ 183
Cdd:PHA02878  223 --------------------------------------------NGASTDARDKCGNTPLHISVGYCKDYDILkLLLEHG 258
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 184 ADINVSRTQDGETALQLAIRNqlPLVVDAICTRGADMSVPDEKGNPPLWLALANNLE-DIASTLVRHGC 251
Cdd:PHA02878  259 VDVNAKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRILISNIC 325
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
407-532 9.88e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 407 DNKGRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKhrQTALHLAA 486
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVH--IRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA--GDLLCTAA 630
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462555837 487 QQDLPTICSVLLENGVDFAAVDENGNNALHLAVMHGRLNNIRVLLT 532
Cdd:PLN03192  631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
Ank_5 pfam13857
Ankyrin repeats (many copies);
471-518 1.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2462555837 471 VNELTKHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLA 518
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
163-399 1.49e-04

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: 45.07  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 163 LLHMAIQRQDSKSALFLLEHQADINVsrtqdGETALqLAIRNQLPLVVDAIctrgADMSVPDEKGNPPLWLALAnnledi 242
Cdd:TIGR00870  56 LFVAAIENENLELTELLLNLSCRGAV-----GDTLL-HAISLEYVDAVEAI----LLHLLAAFRKSGPLELAND------ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 243 astlvRHGCDATcwgpgPGgclQTLLHRAIDENNEPTACFLIRSGCDVN----------SPRQPGAngegeeeaRDGQTP 312
Cdd:TIGR00870 120 -----QYTSEFT-----PG---ITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSF--------YHGESP 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 313 LHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHV--------------AISSQHGVIIQLLVSHPDIHLN-VRDRQGL 377
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLlvmenefkaeyeelSCQMYNFALSLLDKLRDSKELEvILNHQGL 258
                         250       260
                  ....*....|....*....|..
gi 2462555837 378 TPFACAMTFKNNKSAEAILKRE 399
Cdd:TIGR00870 259 TPLKLAAKEGRIVLFRLKLAIK 280
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
308-337 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: 38.78  E-value: 2.22e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462555837 308 DGQTPLHLAASWGLEETVQCLLEFGANVNA 337
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
265-399 2.46e-04

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: 44.41  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 265 QTLLHRAIDENNEPTACFLIRSGCDVNSprqpGANGEGEEEARD------GQTPLHLAASWGLEETVQCLLE---FGANV 335
Cdd:cd22196    95 QTALHIAIERRNMHLVELLVQNGADVHA----RASGEFFKKKKGgpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADI 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 336 NAQDAEGRTPIH--VAISSQ------------HGVIIQLLVSHPDIHL-NVRDRQGLTPFACAMTFKNNKSAEAILKRE 399
Cdd:cd22196   171 SARDSMGNTVLHalVEVADNtpentkfvtkmyNEILILGAKIRPLLKLeEITNKKGLTPLKLAAKTGKIGIFAYILGRE 249
PHA02736 PHA02736
Viral ankyrin protein; Provisional
307-383 3.47e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 307 RDGQTPLHLAASWGL---EETVQCLLEFGANVNAQDA-EGRTPIHVAISSQHGVIIQLLVSHPDIHLNVRDRQGLTPFAC 382
Cdd:PHA02736   53 RHGKQCVHIVSNPDKadpQEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYV 132

                  .
gi 2462555837 383 A 383
Cdd:PHA02736  133 A 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
307-349 3.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462555837 307 RDGQTPLHLAASWGLEETVQCLLEFGANVNAQDAEGRTPIHVA 349
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
314-383 4.42e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 4.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 314 HLAASwGLEETVQCLLEFGANVNAQDAEGRTPIHVAISSQH-GVIIQLLVSHPDIHLnvRDRQGLTPFACA 383
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTL--LDKDGKTPLELA 155
PHA02875 PHA02875
ankyrin repeat protein; Provisional
43-253 4.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  43 NLTAELLQQGANPNLQTEEALPLPKEAASLTslaDSVHLQTPL-HMAIA-YNHPDVVS----VILEQKANALHATNNL-Q 115
Cdd:PHA02875   16 DIARRLLDIGINPNFEIYDGISPIKLAMKFR---DSEAIKLLMkHGAIPdVKYPDIESelhdAVEEGDVKAVEELLDLgK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 116 IIPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsrtQD-- 193
Cdd:PHA02875   93 FADDVFYKDG--MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI---EDcc 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 194 GETALQLAIRNQLPLVVDAICTRGADmsvPDEKGNPP----LWLALANNLEDIASTLVRHGCDA 253
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGADC 228
PHA02798 PHA02798
ankyrin-like protein; Provisional
241-503 6.24e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 241 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNE-PTACFLIRSGCDVNsprqpgangegeEEARDGQTPLHLAASW 319
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDYKHMlDIVKILIENGADIN------------KKNSDGETPLYCLLSN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 320 GL---EETVQCLLEFGANVNAQDAEGRTPIHVAISSQHGV---IIQLLV-SHPDIHLnVRDRQGLTPFACAMTFKNNKSA 392
Cdd:PHA02798  120 GYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLeKGVDINT-HNNKEKYDTLHCYFKYNIDRID 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 393 EAILKR--ESGAAEQVDNKG--RNFLHVAVQ----NSDIES-VLFLISVHANVNSRvqDASKLTPLHLAVQAGSEIIVRN 463
Cdd:PHA02798  199 ADILKLfvDNGFIINKENKShkKKFMEYLNSllydNKRFKKnILDFIFSYIDINQV--DELGFNPLYYSVSHNNRKIFEY 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2462555837 464 LLLAGAKVNELTKHRQTALHLAAQQDLPTICSVLLENGVD 503
Cdd:PHA02798  277 LLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_5 pfam13857
Ankyrin repeats (many copies);
328-380 6.47e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 6.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 328 LLEFG-ANVNAQDAEGRTPIHVAISSQHGVIIQLLVSHPdIHLNVRDRQGLTPF 380
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
31-225 7.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  31 TPLHTACRHGLANLTAELLQQGANPNLQTE-EALPLPK---EAASLTSLADSVHL---------------QTPLHMAIAY 91
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKnNSTPLHYlsnIKYNLTDVKEIVKLlleyganvnapdnngITPLLYAISK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  92 --NHPDVVSVILEQKANA-LHATNNLQIIPDFSLKDSRDQTVLGLALWTGMHTIAAQ----LLGSGAAINDTMSDGQTLL 164
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVnIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDINAKNrvnyLLSYGVPINIKDVYGFTPL 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 165 HMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLAIRNQLPLVVDAICTRGADMSVPDE 225
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
30-222 9.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837  30 ETPLHTACRHGLANLTAELLQQGanpnlqteealplpkeaasltSLADSVHLQ---TPLHMAIAYNHPDVVSVILEQKAN 106
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLG---------------------KFADDVFYKdgmTPLHLATILKKLDIMKLLIARGAD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 107 alhatnnlqiiPDFSLKDSrdQTVLGLALWTGMHTIAAQLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADI 186
Cdd:PHA02875  128 -----------PDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462555837 187 N-VSRTQDgETALQLAIRNQLPLVVDAICTRGADMSV 222
Cdd:PHA02875  195 DyFGKNGC-VAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02884 PHA02884
ankyrin repeat protein; Provisional
241-349 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 241 DIASTLVRHGCDATCWGPGPGGCLQTLLHRAIDENNEPTACFLIRSGCDVNSPrqpgangegEEEARdgQTPLHLAASWG 320
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRY---------AEEAK--ITPLYISVLHG 115
                          90       100
                  ....*....|....*....|....*....
gi 2462555837 321 LEETVQCLLEFGANVNAQDAEGRTPIHVA 349
Cdd:PHA02884  116 CLKCLEILLSYGADINIQTNDMVTPIELA 144
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
447-569 1.49e-03

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: 42.05  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 447 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG-VDFAAVDENG 511
Cdd:cd22194   143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKEsTDITSQDSRG 222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462555837 512 NNALHLAVM-----HGRLNNIRVLLTECTVDAEAFNL------RGQSPLHILGQYGKenaAAIFDLFLE 569
Cdd:cd22194   223 NTVLHALVTvaedsKTQNDFVKRMYDMILLKSENKNLetirnnEGLTPLQLAAKMGK---AEILKYILS 288
Ank_5 pfam13857
Ankyrin repeats (many copies);
151-201 1.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2462555837 151 AAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVsRTQDGETALQLA 201
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
433-485 1.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 433 HANVNSRVQDASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLA 485
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
447-557 2.43e-03

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: 41.32  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 447 TPLHLAVQAGSEIIVRNLLLAGAKVNELTKHR--------------QTALHLAAQQDLPTICSVLLENG---VDFAAVDE 509
Cdd:cd22193    78 TALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEhqpADIEAQDS 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462555837 510 NGNNALHLAVM---HGRLNNIRV------LLTEC-----TVDAEA-FNLRGQSPLHILGQYGK 557
Cdd:cd22193   158 RGNTVLHALVTvadNTKENTKFVtrmydmILIRGaklcpTVELEEiRNNDGLTPLQLAAKMGK 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
28-57 2.82e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.82e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462555837   28 QGETPLHTACRHGLANLTAELLQQGANPNL 57
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
414-624 3.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 414 LHVAVQNSDIESVLFLISVHAN-VNSRVQDASklTPLHLAVQAGSEIIVRNLLLAGAKVNELTKHRQTALHLAAQQDLPT 492
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETT--TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 493 ICSVLLENGVDFA------------------AVDENGNNA-----LHLAVMHGRLNNIRVLLtECTVDAEAFNLRGQSPL 549
Cdd:PHA02874   83 IIKLLIDNGVDTSilpipciekdmiktildcGIDVNIKDAelktfLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPI 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462555837 550 HILGqygKENAAAIFDLFLEcmpgypldkpdadgstvlllaymkgnanlcraivrSGARLGVNNNQGVNIFNYQV 624
Cdd:PHA02874  162 HIAI---KHNFFDIIKLLLE-----------------------------------KGAYANVKDNNGESPLHNAA 198
PHA02946 PHA02946
ankyin-like protein; Provisional
145-352 3.40e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 145 QLLGSGAAINDTMSDGQTLLHMAIQRQDSKSALFLLEHQADINVSRTQDGETALQLA-IRNQLPLVVDAICTRGADMSVP 223
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSgTDDEVIERINLLVQYGAKINNS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 224 -DEKGNPPLwLALANNLEDIASTLVRHGCDATC---WGpgpggclQTLLHRAIDENN--EPTACFLIRSGCdvnSPRQPG 297
Cdd:PHA02946  137 vDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkFG-------KNHIHRHLMSDNpkASTISWMMKLGI---SPSKPD 205
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462555837 298 angegeeeaRDGQTPLHLAASWGLEET-VQCLLEFGANVNAQDAEGRTPIHVAISS 352
Cdd:PHA02946  206 ---------HDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT 252
Ank_4 pfam13637
Ankyrin repeats (many copies);
410-465 4.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 4.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462555837 410 GRNFLHVAVQNSDIESVLFLISVHANVNsrVQDASKLTPLHLAVQAGSEIIVRNLL 465
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
282-622 5.25e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.11  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 282 FLIRSGCDVNsprqpgangegeeEARDGQTPL--HLAASWGLEETVQCLLEFGANVNAQdAEGRTPIHVAI------SSQ 353
Cdd:PHA02989   21 FLLRTGFDVN-------------EEYRGNSILllYLKRKDVKIKIVKLLIDNGADVNYK-GYIETPLCAVLrnreitSNK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 354 HGVIIQLLVSHpDIHLNVRDRQGLTPFACAMTFKNnksaeailkresgaaeqvdnkgrnflhvaVQNSDIesVLFLISVH 433
Cdd:PHA02989   87 IKKIVKLLLKF-GADINLKTFNGVSPIVCFIYNSN-----------------------------INNCDM--LRFLLSKG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 434 ANVNSrVQDASKLTPLHLAVQAGS--EIIVRNLLLAGAKVNELTK-HRQTALHLAAQQDLPTI----CSVLLENGVDFaa 506
Cdd:PHA02989  135 INVND-VKNSRGYNLLHMYLESFSvkKDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVIsikvIKYLIKKGVNI-- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 507 vdeNGNNALHLAVMHGRLNNIRVLLTECT---------VDAEAFNLRGQSPLHILGQYGKENAaaiFDLFLecMPGYPLD 577
Cdd:PHA02989  212 ---ETNNNGSESVLESFLDNNKILSKKEFkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEA---FNYLL--KLGDDIY 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 2462555837 578 KPDADGSTVLLLAYMKGNANLCRAIVrsgaRLGVNNNQGVNIFNY 622
Cdd:PHA02989  284 NVSKDGDTVLTYAIKHGNIDMLNRIL----QLKPGKYLIKKTFEY 324
Ank_4 pfam13637
Ankyrin repeats (many copies);
266-329 6.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 6.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462555837 266 TLLHRAIDENNEPTACFLIRSGCDVNspRQPGangegeeearDGQTPLHLAASWGLEETVQCLL 329
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN--AVDG----------NGETALHFAASNGNVEVLKLLL 54
PHA02791 PHA02791
ankyrin-like protein; Provisional
442-533 8.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462555837 442 DASKLTPLHLAVQAGSEIIVRNLLLAGAKVNELtkHRQTALHLAAQQDLPTICSVLLENGVDFAAVDENGNNALHLAVMH 521
Cdd:PHA02791   27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLL--ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104
                          90
                  ....*....|..
gi 2462555837 522 GRLNNIRVLLTE 533
Cdd:PHA02791  105 GNMQTVKLFVKK 116
 
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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