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Conserved domains on  [gi|62862424|ref|NP_001015359|]
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uncharacterized protein Dmel_CG41099, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-174 7.10e-48

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


:

Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 166.34  E-value: 7.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   63 TVASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDL-QNDGLAL 141
Cdd:cd18303    8 TVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLtLDDEFLL 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCIR 174
Cdd:cd18303   88 ELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
167-255 3.14e-43

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


:

Pssm-ID: 350576  Cd Length: 89  Bit Score: 151.64  E-value: 3.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  167 VGVRSCIRFYCVAEEVGASTLLEYCSSIISTHWDDLTTDDFQHMSGPLLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKY 246
Cdd:cd18501    1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                 ....*....
gi 62862424  247 GNSLVNTFS 255
Cdd:cd18501   81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1054-1116 1.72e-40

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: 142.95  E-value: 1.72e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862424 1054 ESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15728    1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
741-1034 2.67e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  741 LIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMD 820
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  821 IRGRNFLHLAILKDDLESVLFLLAIQVDVNSRvhDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIE 900
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  901 RGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLtESRVNAEATNLKGRNPLHELCRvvedSTAGLICEL 980
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE----NGNLEIVKL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62862424  981 FLESMPKypINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGINIF 1034
Cdd:COG0666  238 LLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-671 1.18e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  383 LLLKVPNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTNSKTGDSLLQVFALDRHRGEKSAIFLADFADL 462
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  463 DHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHIAVEANAIDALEAFVElknksHDIDFNCQDING 542
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLE-----AGADVNAQDNDG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  543 DSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSE 622
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 62862424  623 VVDALCRRGIALSI-NKNGESPLWSALEKGYEDVAKILVRHGIDTDCWDE 671
Cdd:COG0666  234 IVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
243-392 7.53e-11

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   243 IQKYGnSLVNTFSENGILPLEMALSSK--NAKIAKSLVDNGmANINAVNMEGFSLLKSALKNG--DAFSANFLLDQ---- 314
Cdd:PHA03100   92 LLEYG-ANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKgvdi 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   315 ------NCLLDLPSKPSS-----DTALHIICNYgpdNTPEImevVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKL 383
Cdd:PHA03100  170 naknrvNYLLSYGVPINIkdvygFTPLHYAVYN---NNPEF---VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|
gi 62862424   384 LLKV-PNIDI 392
Cdd:PHA03100  244 LLNNgPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
644-752 1.08e-07

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    644 LWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDENKESVAIFLIqsqcdldssrqpgpNGEGGDEAQDKA 723
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK----NGRTALHLAAKNGHLEIVKLLL--------------EHADVNLKDNGR 62
                           90       100
                   ....*....|....*....|....*....
gi 62862424    724 SPLHLCCHWGQTKVLQTLIDHGANVNLID 752
Cdd:pfam12796   63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-174 7.10e-48

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 166.34  E-value: 7.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   63 TVASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDL-QNDGLAL 141
Cdd:cd18303    8 TVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLtLDDEFLL 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCIR 174
Cdd:cd18303   88 ELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
167-255 3.14e-43

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


Pssm-ID: 350576  Cd Length: 89  Bit Score: 151.64  E-value: 3.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  167 VGVRSCIRFYCVAEEVGASTLLEYCSSIISTHWDDLTTDDFQHMSGPLLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKY 246
Cdd:cd18501    1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                 ....*....
gi 62862424  247 GNSLVNTFS 255
Cdd:cd18501   81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1054-1116 1.72e-40

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: 142.95  E-value: 1.72e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862424 1054 ESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15728    1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
741-1034 2.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  741 LIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMD 820
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  821 IRGRNFLHLAILKDDLESVLFLLAIQVDVNSRvhDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIE 900
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  901 RGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLtESRVNAEATNLKGRNPLHELCRvvedSTAGLICEL 980
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE----NGNLEIVKL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62862424  981 FLESMPKypINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGINIF 1034
Cdd:COG0666  238 LLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-671 1.18e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  383 LLLKVPNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTNSKTGDSLLQVFALDRHRGEKSAIFLADFADL 462
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  463 DHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHIAVEANAIDALEAFVElknksHDIDFNCQDING 542
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLE-----AGADVNAQDNDG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  543 DSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSE 622
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 62862424  623 VVDALCRRGIALSI-NKNGESPLWSALEKGYEDVAKILVRHGIDTDCWDE 671
Cdd:COG0666  234 IVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
214-501 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  214 LLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKYGNSLVNTFSENGILPLEMALSSKNAKIAKSLVDNGmANINAVNMEGF 293
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG-ADINAKDDGGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  294 SLLKSALKNGDAFSANFLLDQNCLLDLPSKpSSDTALHIICNYGpdntpeIMEVVKKILQRQLNINIQNIKGETPLHIAI 373
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNG------NLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  374 ARRNVEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEflIASILLSMGARTDRTNSKTGDSLLqvFALDRHRGEKSA 453
Cdd:COG0666  162 ANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLE--IVKLLLEAGADVNAKDNDGKTALD--LAAENGNLEIVK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 62862424  454 IFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHID 501
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1058-1117 9.20e-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: 89.75  E-value: 9.20e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62862424   1058 AESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPIL-KFGINKPVRVCTVCFNVLQ 1117
Cdd:pfam01363    7 SSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1059-1117 4.01e-21

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: 87.87  E-value: 4.01e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424    1059 ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVLQ 1117
Cdd:smart00064    9 EVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENLN 67
PHA02878 PHA02878
ankyrin repeat protein; Provisional
725-1046 2.71e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   725 PLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILlchpdIDLKLRDKSGNTPFA--TALDFRNH 802
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM-----IRSINKCSVFYTLVAikDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   803 NAAQRIL-DRFPTAAEQMDIRGRNFLHLAILkdDLESVLFLLAIQVDVNSRVHDANqSSPLHLAAASQNEMITRNLILAG 881
Cdd:PHA02878  115 EIFKIILtNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKG-NTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   882 ARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAV-RCAQFFIVRELLTE-SRVNAEATnLKGR 959
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHgVDVNAKSY-ILGL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   960 NPLHELCRvVEDSTaglicELFLESmpKYPINIPDMDGNTPLLLSFM-RGQSPLCKILVKAGACLGTENKDGINIFNFKL 1038
Cdd:PHA02878  271 TALHSSIK-SERKL-----KLLLEY--GADINSLNSYKLTPLSSAVKqYLCINIGRILISNICLLKRIKPDIKNSEGFID 342

                  ....*...
gi 62862424  1039 ATDQLLHN 1046
Cdd:PHA02878  343 NMDCITSN 350
PHA03100 PHA03100
ankyrin repeat protein; Provisional
346-609 2.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   346 EVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVpNIDINLRTYDEKCALELsLSMGDHEFL----IASILL 421
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDN-GADINSSTKNNSTPLHY-LSNIKYNLTdvkeIVKLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   422 SMGARTDRTNSKTGDSLLqvFALDRHRGEKSAI--FLADFADLDHINFRGLTALHIAALNNMPNL--VKKLIVNGassnl 497
Cdd:PHA03100   94 EYGANVNAPDNNGITPLL--YAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKG----- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   498 khidcglksalhiaVEANAIDALEAFVelknkSHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLS 577
Cdd:PHA03100  167 --------------VDINAKNRVNYLL-----SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 62862424   578 PLHQSIKNEDSDISLFLLEQGADITALTENLD 609
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPSIKTIIETLL 259
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
67-166 1.65e-12

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 64.97  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424     67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTD-LIDLQNdglA 140
Cdd:pfam00651    4 LREQGELCDVTLVVGDKEFRAHKAVLAACSPYFkalfsGQESESSVSEITLDDVSPEDFEALLEFMYTGkLISEEN---V 80
                           90       100
                   ....*....|....*....|....*.
gi 62862424    141 LDLLKAAHRFGLPSLLGICERALVTS 166
Cdd:pfam00651   81 DDLLAAADKLQIPSLVDKCEEFLIKS 106
Ank_2 pfam12796
Ankyrin repeats (3 copies);
862-944 1.14e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    862 LHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIqNNADYDATDaDGNNALHIAVRCAQFFIVR 941
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ...
gi 62862424    942 ELL 944
Cdd:pfam12796   79 LLL 81
PHA02876 PHA02876
ankyrin repeat protein; Provisional
561-900 2.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   561 LIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRgiALSINKNG 640
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN--RSNINKND 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   641 ESpLWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDENKESVAI-FLIQSQCDLDSSRQPGpngeggdea 719
Cdd:PHA02876  242 LS-LLKAIRNEDLETSLLLYDAGFSVNSIDD----CKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKG--------- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   720 qdkASPLHLCCHWG-QTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALd 798
Cdd:PHA02876  308 ---ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAA- 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   799 FRNHNAAQRILDRFPTAAEQMDIRGRNFLHLAIL-KDDLESVLFLLAIQVDVNSRVHDAnqSSPLHLAAASQNEM-ITRN 876
Cdd:PHA02876  384 VRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDL--STPLHYACKKNCKLdVIEM 461
                         330       340
                  ....*....|....*....|....
gi 62862424   877 LILAGARMNERDAVQKLPLHIAIE 900
Cdd:PHA02876  462 LLDNGADVNAINIQNQYPLLIALE 485
PHA03100 PHA03100
ankyrin repeat protein; Provisional
243-392 7.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   243 IQKYGnSLVNTFSENGILPLEMALSSK--NAKIAKSLVDNGmANINAVNMEGFSLLKSALKNG--DAFSANFLLDQ---- 314
Cdd:PHA03100   92 LLEYG-ANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKgvdi 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   315 ------NCLLDLPSKPSS-----DTALHIICNYgpdNTPEImevVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKL 383
Cdd:PHA03100  170 naknrvNYLLSYGVPINIkdvygFTPLHYAVYN---NNPEF---VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|
gi 62862424   384 LLKV-PNIDI 392
Cdd:PHA03100  244 LLNNgPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
330-431 1.20e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    330 LHIICNYGPdntpeiMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDInlrTYDEKCALELSLSM 409
Cdd:pfam12796    1 LHLAAKNGN------LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
                           90       100
                   ....*....|....*....|..
gi 62862424    410 GDHEflIASILLSMGARTDRTN 431
Cdd:pfam12796   72 GHLE--IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
579-665 1.29e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    579 LHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRgIALSINKNGESPLWSALEKGYEDVAKI 658
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                   ....*..
gi 62862424    659 LVRHGID 665
Cdd:pfam12796   80 LLEKGAD 86
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
75-166 1.45e-08

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 53.46  E-value: 1.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424      75 DIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWS-----DLNEDVVLSLLRWIYTDLIDLqNDGLALDLLKAAHR 149
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSeiyldDVSPEDFRALLNFLYTGKLDL-PEENVEELLELADY 79
                            90
                    ....*....|....*..
gi 62862424     150 FGLPSLLGICERALVTS 166
Cdd:smart00225   80 LQIPGLVELCEEFLLKL 96
Ank_2 pfam12796
Ankyrin repeats (3 copies);
644-752 1.08e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    644 LWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDENKESVAIFLIqsqcdldssrqpgpNGEGGDEAQDKA 723
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK----NGRTALHLAAKNGHLEIVKLLL--------------EHADVNLKDNGR 62
                           90       100
                   ....*....|....*....|....*....
gi 62862424    724 SPLHLCCHWGQTKVLQTLIDHGANVNLID 752
Cdd:pfam12796   63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
275-385 5.87e-06

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: 50.46  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    275 KSLVDNGMANINAVNMEGFSLLKSALKNGDAFS-ANFLLDQNCLLDLpskpsSDTALHIICNYGPDNTPEIMEVVKKILQ 353
Cdd:TIGR00870   35 RDLEEPKKLNINCPDRLGRSALFVAAIENENLElTELLLNLSCRGAV-----GDTLLHAISLEYVDAVEAILLHLLAAFR 109
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 62862424    354 RQLNINIQN-------IKGETPLHIAIARRNVEMVKLLL 385
Cdd:TIGR00870  110 KSGPLELANdqytsefTPGITALHLAAHRQNYEIVKLLL 148
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
823-932 1.73e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  823 GRNFLHLAILKDDLESVLFLLA-----IQVDVNSRVHDAnqSSPLHLAAASQNEMITRNLILAGARMNE--------RDA 889
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQG--ETALHIAVVNQNLNLVRELIARGADVVSpratgtffRPG 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 62862424  890 VQKL------PLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAV 932
Cdd:cd22192  129 PKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177
PHA02875 PHA02875
ankyrin repeat protein; Provisional
582-775 4.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   582 SIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKNG-ESPLWSALEKGYEDVAKILV 660
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   661 RHG--IDTDCWDEGpegcrQTLLHRAIDENKESVAIFLIQSQCDLDSSrqpgpngeggdeAQDKASPLHLCCHWGQTKVL 738
Cdd:PHA02875   89 DLGkfADDVFYKDG-----MTPLHLATILKKLDIMKLLIARGADPDIP------------NTDKFSPLHLAVMMGDIKGI 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 62862424   739 QTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILL 775
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
366-494 1.67e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  366 ETPLHIAIARRNVEMVKLLLKVPNIDINLRtydekcalelslsmgdhefliasillsmGArtdrtnskTGDSLLQVFALD 445
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQR----------------------------GA--------LGETALHVAALY 61
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424  446 RHRgeKSAIFLADfADLDHIN-------FRGLTALHIAALNNMPNLVKKLIVNGAS 494
Cdd:cd22192   62 DNL--EAAVVLME-AAPELVNepmtsdlYQGETALHIAVVNQNLNLVRELIARGAD 114
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
372-498 1.76e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    372 AIARRNVEMVKLLLKVP-NIDINLRTYDEKCALELSLSMGDHEFLIaSILLSMGARTDrtnskTGDSLLQVFALDRHRGE 450
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPkKLNINCPDRLGRSALFVAAIENENLELT-ELLLNLSCRGA-----VGDTLLHAISLEYVDAV 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    451 KSAIFLADFADLDHIN------------FRGLTALHIAALNNMPNLVKKLIVNGASSNLK 498
Cdd:TIGR00870   98 EAILLHLLAAFRKSGPlelandqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
721-750 4.12e-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: 4.12e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 62862424     721 DKASPLHLCCHWGQTKVLQTLIDHGANVNL 750
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
339-385 4.18e-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: 41.28  E-value: 4.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424  339 DNTPEIMEVV------KKILQRQLNINI--QNIKGETPLHIAIARRNVEMVKLLL 385
Cdd:cd22194  107 ENTKEIVRILlafaeeNGILDRFINAEYteEAYEGQTALNIAIERRQGDIVKLLI 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
364-392 8.20e-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: 34.87  E-value: 8.20e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 62862424     364 KGETPLHIAIARRNVEMVKLLL-KVPNIDI 392
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLdKGADINA 30
 
Name Accession Description Interval E-value
BTB_POZ_Rank-5 cd18303
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-174 7.10e-48

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1) or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms. It contains an N-terminal BTB domain, followed by a BACK domain, several ankyrin (ANK) repeats and a C-terminal FYVE domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349612 [Multi-domain]  Cd Length: 120  Bit Score: 166.34  E-value: 7.10e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   63 TVASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDL-QNDGLAL 141
Cdd:cd18303    8 TVASLFDKELYSDITIKLADKSIPAHKFVLAARSEKWSNENLASTNELDLSDISYEVVLALLRWLYTDELDLtLDDEFLL 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCIR 174
Cdd:cd18303   88 ELMKAAKRFQLTDLVERCERALMSSVNVDNCIR 120
BACK_ANKFY1_Rank5 cd18501
BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ...
167-255 3.14e-43

BACK (BTB and C-terminal Kelch) domain found in rabankyrin-5 (Rank-5); Rank-5, also called ankyrin repeat and FYVE domain-containing protein 1 (ANKFY1), or ankyrin repeats hooked to a zinc finger motif (ANKHZN), is a Rab5 effector that regulates and coordinates different endocytic mechanisms.


Pssm-ID: 350576  Cd Length: 89  Bit Score: 151.64  E-value: 3.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  167 VGVRSCIRFYCVAEEVGASTLLEYCSSIISTHWDDLTTDDFQHMSGPLLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKY 246
Cdd:cd18501    1 VNVRNCIRFYQTAEEIGASTLREYCSEIISTHWDDLTPEDFAKMSAPLLYRMFKSKTKHPLHAAIRLKREDVVFLYLIEF 80

                 ....*....
gi 62862424  247 GNSLVNTFS 255
Cdd:cd18501   81 DSQLPGKLN 89
FYVE_ANFY1 cd15728
FYVE domain found in ankyrin repeat and FYVE domain-containing protein 1 (ANFY1) and similar ...
1054-1116 1.72e-40

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: 142.95  E-value: 1.72e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862424 1054 ESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15728    1 EPPWADGDYCYECGVKFGITTRKHHCRHCGRLLCSKCSTKEVPIIKFDLNKPVRVCDVCFDVL 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
741-1034 2.67e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  741 LIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMD 820
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  821 IRGRNFLHLAILKDDLESVLFLLAIQVDVNSRvhDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIE 900
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  901 RGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLtESRVNAEATNLKGRNPLHELCRvvedSTAGLICEL 980
Cdd:COG0666  163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAE----NGNLEIVKL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62862424  981 FLESMPKypINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGINIF 1034
Cdd:COG0666  238 LLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
383-671 1.18e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 1.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  383 LLLKVPNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTNSKTGDSLLQVFALDRHRGEKSAIFLADFADL 462
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  463 DHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHIAVEANAIDALEAFVElknksHDIDFNCQDING 542
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLE-----AGADVNAQDNDG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  543 DSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSE 622
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 62862424  623 VVDALCRRGIALSI-NKNGESPLWSALEKGYEDVAKILVRHGIDTDCWDE 671
Cdd:COG0666  234 IVKLLLEAGADLNAkDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
587-928 1.35e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  587 DSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKNGESPLWSALEKGYEDVAKILVRHGIDT 666
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  667 DCWDEGpegcRQTLLHRAIDENKESVAIFLIQSQCDLDSSRQPGpngeggdeaqdkASPLHLCCHWGQTKVLQTLIDHGA 746
Cdd:COG0666   81 NAKDDG----GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG------------ETPLHLAAYNGNLEIVKLLLEAGA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  747 NVNLIDAESKSPLHVAIESQYDEIISILLCHpDIDLKLRDKSGNTPfataldfrnhnaaqrildrfptaaeqmdirgrnf 826
Cdd:COG0666  145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETP---------------------------------- 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  827 LHLAILKDDLESVLFLLAIQVDVNSRvhDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPA 906
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAK--DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267
                        330       340
                 ....*....|....*....|..
gi 62862424  907 VSALIQNNADYDATDADGNNAL 928
Cdd:COG0666  268 VKLLLLALLLLAAALLDLLTLL 289
FYVE_Hrs cd15720
FYVE domain found in hepatocyte growth factor (HGF)-regulated tyrosine kinase substrate (Hrs) ...
1057-1116 1.08e-22

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: 92.06  E-value: 1.08e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424 1057 WAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15720    2 WKDGDECHRCRVQFGVFQRKHHCRACGQVFCGKCSSKSSTIPKFGIEKEVRVCDPCYEKL 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
214-501 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 1.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  214 LLFEMLKTKTKHPLHAAVRLLREDVVSLCIQKYGNSLVNTFSENGILPLEMALSSKNAKIAKSLVDNGmANINAVNMEGF 293
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG-ADINAKDDGGN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  294 SLLKSALKNGDAFSANFLLDQNCLLDLPSKpSSDTALHIICNYGpdntpeIMEVVKKILQRQLNINIQNIKGETPLHIAI 373
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNG------NLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  374 ARRNVEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEflIASILLSMGARTDRTNSKTGDSLLqvFALDRHRGEKSA 453
Cdd:COG0666  162 ANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLE--IVKLLLEAGADVNAKDNDGKTALD--LAAENGNLEIVK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 62862424  454 IFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHID 501
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
1058-1117 9.20e-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: 89.75  E-value: 9.20e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62862424   1058 AESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPIL-KFGINKPVRVCTVCFNVLQ 1117
Cdd:pfam01363    7 SSATVCMICSKPFTFFRRRHHCRNCGRVFCSACSSKKISLLpELGSNKPVRVCDACYDTLQ 67
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
351-639 2.13e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.79  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  351 ILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDINLRtyDEKCALELSLSMGDHEFLIASILLSMGARTDRT 430
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA--DALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  431 NSKTGDSLLqvFALDRHRGEKSAIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHI 510
Cdd:COG0666   84 DDGGNTLLH--AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  511 AVEANAIDALEAFVElknksHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDI 590
Cdd:COG0666  160 AAANGNLEIVKLLLE-----AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62862424  591 SLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKN 639
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
1059-1117 4.01e-21

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: 87.87  E-value: 4.01e-21
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424    1059 ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVLQ 1117
Cdd:smart00064    9 EVSNCMGCGKEFNLTKRRHHCRNCGRIFCSKCSSKKAPLPKLGIERPVRVCDDCYENLN 67
FYVE_LST2 cd15731
FYVE domain found in lateral signaling target protein 2 homolog (Lst2) and similar proteins; ...
1052-1114 6.91e-21

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: 87.40  E-value: 6.91e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862424 1052 PQESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFN 1114
Cdd:cd15731    3 PLWVPDEACPQCMACSAPFTVLRRRHHCRNCGKIFCSRCSSNSVPLPRYGQMKPVRVCNHCFM 65
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
282-612 1.14e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.87  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  282 MANINAVNMEGFSLLKSALKNGDAFSANFLLDQNCLLDLPSKPSSDTALHIICNYGPDNTPEIMEVVKKILQRQLNINIQ 361
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  362 NIKGETPLHIAIARRNVEMVKLLLKvPNIDINLRTYDEKCALELSLSMGDHEflIASILLSMGArtdrtnsktgdsllqv 441
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLE--IVKLLLEAGA---------------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  442 faldrhrgeksaifladfaDLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHIAVEANAIDALE 521
Cdd:COG0666  145 -------------------DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR--DNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  522 AFVElknksHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADI 601
Cdd:COG0666  204 LLLE-----AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                        330
                 ....*....|.
gi 62862424  602 TALTENLDSAL 612
Cdd:COG0666  279 AAALLDLLTLL 289
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
1061-1116 3.80e-20

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: 85.13  E-value: 3.80e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424 1061 DYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15719   10 DSCTGCSVRFSLTERRHHCRNCGQLFCSKCSRFESEIRRLRISRPVRVCQACYNIL 65
FYVE_spVPS27p_like cd15735
FYVE domain found in Schizosaccharomyces pombe vacuolar protein sorting-associated protein 27 ...
1057-1113 2.57e-19

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: 82.58  E-value: 2.57e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424 1057 WAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15735    3 WVDSDVCMRCRTAFTFTNRKHHCRNCGGVFCQQCSSKSLPLPHFGINQPVRVCDGCY 59
PHA02878 PHA02878
ankyrin repeat protein; Provisional
725-1046 2.71e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   725 PLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILlchpdIDLKLRDKSGNTPFA--TALDFRNH 802
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM-----IRSINKCSVFYTLVAikDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   803 NAAQRIL-DRFPTAAEQMDIRGRNFLHLAILkdDLESVLFLLAIQVDVNSRVHDANqSSPLHLAAASQNEMITRNLILAG 881
Cdd:PHA02878  115 EIFKIILtNRYKNIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKG-NTALHYATENKDQRLTELLLSYG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   882 ARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAV-RCAQFFIVRELLTE-SRVNAEATnLKGR 959
Cdd:PHA02878  192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHgVDVNAKSY-ILGL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   960 NPLHELCRvVEDSTaglicELFLESmpKYPINIPDMDGNTPLLLSFM-RGQSPLCKILVKAGACLGTENKDGINIFNFKL 1038
Cdd:PHA02878  271 TALHSSIK-SERKL-----KLLLEY--GADINSLNSYKLTPLSSAVKqYLCINIGRILISNICLLKRIKPDIKNSEGFID 342

                  ....*...
gi 62862424  1039 ATDQLLHN 1046
Cdd:PHA02878  343 NMDCITSN 350
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
1054-1112 9.17e-19

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: 81.27  E-value: 9.17e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424 1054 ESPWA---ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVC 1112
Cdd:cd15727    1 EPPWVpdkECPVCMSCKKKFDFFKRRHHCRRCGKCFCSDCCSNKVPLPRMCFVDPVRVCNEC 62
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
1063-1113 4.14e-18

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: 79.11  E-value: 4.14e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd00065    2 CMLCGKKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPVRVCDSCY 52
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
1056-1116 1.27e-17

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: 78.16  E-value: 1.27e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1056 PWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCsCNDVPILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15729    9 PDSEAPNCMQCEVKFTFTKRRHHCRACGKVLCSAC-CSLKARLEYLDNKEARVCVPCYQTL 68
PHA03095 PHA03095
ankyrin-like protein; Provisional
558-944 6.77e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 6.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   558 VPTLIRGGSDVNGKNKNNLSPLHQSIKN---EDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEvvdalcrrgial 634
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL------------ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   635 sinkngesplwsalekgyeDVAKILVRHGIDTDCWDegpeGCRQTLLHraidenkesvaifliqsqcdldssrqpgpnge 714
Cdd:PHA03095   98 -------------------DVIKLLIKAGADVNAKD----KVGRTPLH-------------------------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   715 ggdeaqdkaspLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQ--YDEIISILLCHpDIDLKLRDKSGNTP 792
Cdd:PHA03095  123 -----------VYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDA-GADVYAVDDRFRSL 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   793 FATALD-FRNHNAAQRILDRFPTAAEQMDIRGRNFLH-LAILKDDLES-VLFLLAIQVDVNSRvhDANQSSPLHLAAASQ 869
Cdd:PHA03095  191 LHHHLQsFKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSSCKRSlVLPLLIAGISINAR--NRYGQTPLHYAAVFN 268
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62862424   870 NEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDAD---GNNALHIAVRCAQFFIVRELL 944
Cdd:PHA03095  269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATlntASVAGGDIPSDATRLCVAKVV 346
FYVE_WDFY1_like cd15718
FYVE domain found in WD40 repeat and FYVE domain-containing protein WDFY1 and WDFY2, and ...
1056-1113 1.57e-16

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: 75.05  E-value: 1.57e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424 1056 PWAESDYCQHCTNRF-----------TITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15718    2 EWAESDNCQKCSRPFfwnfkqmwekkTLGVRQHHCRKCGKAVCDKCSSNRSTIPVMGFEFPVRVCNECY 70
PHA03100 PHA03100
ankyrin repeat protein; Provisional
346-609 2.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   346 EVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVpNIDINLRTYDEKCALELsLSMGDHEFL----IASILL 421
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDN-GADINSSTKNNSTPLHY-LSNIKYNLTdvkeIVKLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   422 SMGARTDRTNSKTGDSLLqvFALDRHRGEKSAI--FLADFADLDHINFRGLTALHIAALNNMPNL--VKKLIVNGassnl 497
Cdd:PHA03100   94 EYGANVNAPDNNGITPLL--YAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKG----- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   498 khidcglksalhiaVEANAIDALEAFVelknkSHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLS 577
Cdd:PHA03100  167 --------------VDINAKNRVNYLL-----SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 62862424   578 PLHQSIKNEDSDISLFLLEQGADITALTENLD 609
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPSIKTIIETLL 259
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1056-1113 7.42e-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: 7.42e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424 1056 PWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFG-INKPVRVCTVCF 1113
Cdd:cd15760    1 HWKPDSRCDVCRKKFGLFKRRHHCRNCGDSFCSEHSSRRIPLPHLGpLGVPQRVCDRCF 59
PHA02874 PHA02874
ankyrin repeat protein; Provisional
720-963 1.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   720 QDKASPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLchpdidlklrDKSGNTPFATALDF 799
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI----------DNGVDTSILPIPCI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   800 rNHNAAQRILDrfptAAEQMDIRGR---NFLHLAILKDDLESVLFLLAIQVDVNsrVHDANQSSPLHLAAASQNEMITRN 876
Cdd:PHA02874  103 -EKDMIKTILD----CGIDVNIKDAelkTFLHYAIKKGDLESIKMLFEYGADVN--IEDDNGCYPIHIAIKHNFFDIIKL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   877 LILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIvrELLTESRvNAEATNL 956
Cdd:PHA02874  176 LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNA-SINDQDI 252

                  ....*..
gi 62862424   957 KGRNPLH 963
Cdd:PHA02874  253 DGSTPLH 259
FYVE_EEA1 cd15730
FYVE domain found in early endosome antigen 1 (EEA1) and similar proteins; EEA1, also termed ...
1056-1116 2.61e-15

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: 71.28  E-value: 2.61e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62862424 1056 PWA---ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFgiNKPVRVCTVCFNVL 1116
Cdd:cd15730    2 KWAddeEVQNCMACGKGFSVTVRKHHCRQCGNIFCNECSSKTATTPSS--KKPVRVCDACFDDL 63
FYVE_RUFY1_like cd15721
FYVE domain found in RUN and FYVE domain-containing protein RUFY1, RUFY2 and similar proteins; ...
1063-1113 4.31e-15

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: 70.49  E-value: 4.31e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGinKPVRVCTVCF 1113
Cdd:cd15721   10 CQQCEKEFSLSRRKHHCRNCGGIFCNSCSDNTMPLPSSA--KPVRVCDTCY 58
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
1063-1113 6.26e-15

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: 70.16  E-value: 6.26e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPiLKFGINKPVRVCTVCF 1113
Cdd:cd15743   12 CMICTSEFTVTWRRHHCRACGKVVCGSCSSNKAP-LEYLKNKSARVCDECF 61
FYVE_PKHF cd15717
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1), 2 (phafin-2), ...
1056-1113 1.03e-14

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: 69.70  E-value: 1.03e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424 1056 PWAESDYCQHCTN-RFTITMRKHHCRHCGRVLCSKCSCNDVpILKFGINKPVRVCTVCF 1113
Cdd:cd15717    4 PDSEAPVCMHCKKtKFTAINRRHHCRKCGAVVCGACSSKKF-LLPHQSSKPLRVCDTCY 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
226-634 1.09e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.95  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   226 PLHAAVRLLREDVVSLCIQkYGNSlVNTFSENGILPLEMALSSKNAKIAKSLVDNgMANINAVNMegfSLLKsALKNGDA 305
Cdd:PHA02876  181 PIHYAAERGNAKMVNLLLS-YGAD-VNIIALDDLSVLECAVDSKNIDTIKAIIDN-RSNINKNDL---SLLK-AIRNEDL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   306 FSANFLLDQNCLLDlPSKPSSDTALHIICNygpdnTPEIMEVVKKILQRQLNINIQNIKGETPLHiaiarrnvemvkLLL 385
Cdd:PHA02876  254 ETSLLLYDAGFSVN-SIDDCKNTPLHHASQ-----APSLSRLVPKLLERGADVNAKNIKGETPLY------------LMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   386 KVPNIDINLRTydekcalelslsmgdhefliasiLLSMGARTDRTNSKTGDSLLQVFALDRHRgeKSAIFLADF-ADLDH 464
Cdd:PHA02876  316 KNGYDTENIRT-----------------------LIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLELgANVNA 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   465 INFRGLTALHIAALNNMPNLVKKLIVNGAssNLKHIDCGLKSALHIAveanaidaleafvelknkshdidfncqdINGDS 544
Cdd:PHA02876  371 RDYCDKTPIHYAAVRNNVVIINTLLDYGA--DIEALSQKIGTALHFA----------------------------LCGTN 420
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   545 PLslclslkrtTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNE-DSDISLFLLEQGADITALteNLDSALDLSIKHDLSEV 623
Cdd:PHA02876  421 PY---------MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI--NIQNQYPLLIALEYHGI 489
                         410
                  ....*....|.
gi 62862424   624 VDALCRRGIAL 634
Cdd:PHA02876  490 VNILLHYGAEL 500
FYVE_RUFY1 cd15758
FYVE domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
1059-1116 1.25e-14

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: 69.71  E-value: 1.25e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62862424 1059 ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFgiNKPVRVCTVCFNVL 1116
Cdd:cd15758   11 EATHCKQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSY--PKPVRVCDSCHTLL 66
PHA03100 PHA03100
ankyrin repeat protein; Provisional
259-540 2.07e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   259 ILPLEMALSSKNAKIAKSLVDNGmANINAVNMegfsllksalkngdafsanflldqnclldlpskpSSDTALHIICNYgP 338
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNG-ADINSSTK----------------------------------NNSTPLHYLSNI-K 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   339 DNTPEIMEVVKKILQRQLNINIQNIKGETPLHIAIARR--NVEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEFLI 416
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKIDLKI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   417 ASILLSMGARTDRTNSktgdsllqvfaLDrhrgeksaIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSN 496
Cdd:PHA03100  159 LKLLIDKGVDINAKNR-----------VN--------YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 62862424   497 LKHIDCglKSALHIAVEANaidALEAFVELKNKSHDIDFNCQDI 540
Cdd:PHA03100  220 LVNKYG--DTPLHIAILNN---NKEIFKLLLNNGPSIKTIIETL 258
FYVE_RABE_unchar cd15739
FYVE domain found in uncharacterized rab GTPase-binding effector proteins from bilateria; This ...
1061-1117 4.68e-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: 4.68e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424 1061 DYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPilKFGINKPVRVCTVCFNVLQ 1117
Cdd:cd15739   11 DQCPNCKTPFSVGKRKHHCRHCGKIFCSDCLTKTVP--SGPNRRPARVCDVCHTLLV 65
PHA02876 PHA02876
ankyrin repeat protein; Provisional
724-1023 7.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   724 SPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQ-YDEIISILLCHPDI---DLKLRDKSGNTPFATAL-- 797
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnIDTIKAIIDNRSNInknDLSLLKAIRNEDLETSLll 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   798 -----------DFRN---HNAAQ---------RILDRfPTAAEQMDIRGRNFLHLAILKD-DLESVLFLLAIQVDVNSRv 853
Cdd:PHA02876  260 ydagfsvnsidDCKNtplHHASQapslsrlvpKLLER-GADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAA- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   854 hDANQSSPLHLAAA-SQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAV 932
Cdd:PHA02876  338 -DRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   933 RCAQFFIVRELLTESRVNAEATNLKGRNPLHELCRvveDSTAGLICELFLESMPKypINIPDMDGNTPLLLSFmrGQSPL 1012
Cdd:PHA02876  417 CGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACK---KNCKLDVIEMLLDNGAD--VNAINIQNQYPLLIAL--EYHGI 489
                         330
                  ....*....|.
gi 62862424  1013 CKILVKAGACL 1023
Cdd:PHA02876  490 VNILLHYGAEL 500
BTB_POZ_trishanku-like cd18314
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
73-159 2.77e-13

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in Dictyostelium discoideum trishanku and similar proteins; Trishanku is a novel regulator required for normal morphogenesis and cell-type stability in Dictyostelium discoideum. It contains a BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349623 [Multi-domain]  Cd Length: 96  Bit Score: 66.60  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   73 YADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGLaLDLLKAA 147
Cdd:cd18314    6 FSDVVLCVGDRKFFAHRIVLCARSPVFrsmltGSMIESNLKEVTLEDVEPEIFETVLKYMYTGQVTLSEENV-LDLLMLA 84
                         90
                 ....*....|..
gi 62862424  148 HRFGLPSLLGIC 159
Cdd:cd18314   85 SKYQVPDLEKLC 96
FYVE_WDFY1 cd15756
FYVE domain found in WD40 repeat and FYVE domain-containing protein 1 (WDFY1) and similar ...
1052-1117 5.00e-13

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: 65.48  E-value: 5.00e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424 1052 PQespWAESDYCQHCTNRF-----------TITMRKHHCRHCGRVLCSKCSC--NDVPILKFGINkpVRVCTVCFNVLQ 1117
Cdd:cd15756    1 PQ---WLESDSCQKCEQPFfwnikqmwdtkTLGLRQHHCRKCGQAVCGKCSSkrSSYPIMGFEFQ--VRVCDSCFETIK 74
PHA03095 PHA03095
ankyrin-like protein; Provisional
736-1021 1.28e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   736 KVLQTLIDHGANVNLIDAESKSPLHV---AIESQYDEIISILLcHPDIDLKLRDKSGNTPfataldfrnhnaaqrildrf 812
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLL-EAGADVNAPERCGFTP-------------------- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   813 ptaaeqmdirgrnfLHLAILKDDLESVL-FLLAIQVDVNSRvhDANQSSPLH--LAAASQNEMITRNLILAGARMNERDA 889
Cdd:PHA03095   87 --------------LHLYLYNATTLDVIkLLIKAGADVNAK--DKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   890 VQKLPLHIAIERGNLPA--VSALIQNNADYDATDADGNNALHIAvrcAQFF-----IVRELlTESRVNAEATNLKGRNPL 962
Cdd:PHA03095  151 YGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHH---LQSFkprarIVREL-IRAGCDPAATDMLGNTPL 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424   963 HELcrVVEDSTAGLICELFLESMPKypINIPDMDGNTPLLLSFMRGQSPLCKILVKAGA 1021
Cdd:PHA03095  227 HSM--ATGSSCKRSLVLPLLIAGIS--INARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
BTB pfam00651
BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain ...
67-166 1.65e-12

BTB/POZ domain; The BTB (for BR-C, ttk and bab) or POZ (for Pox virus and Zinc finger) domain is present near the N-terminus of a fraction of zinc finger (pfam00096) proteins and in proteins that contain the pfam01344 motif such as Kelch and a family of pox virus proteins. The BTB/POZ domain mediates homomeric dimerization and in some instances heteromeric dimerization. The structure of the dimerized PLZF BTB/POZ domain has been solved and consists of a tightly intertwined homodimer. The central scaffolding of the protein is made up of a cluster of alpha-helices flanked by short beta-sheets at both the top and bottom of the molecule. POZ domains from several zinc finger proteins have been shown to mediate transcriptional repression and to interact with components of histone deacetylase co-repressor complexes including N-CoR and SMRT. The POZ or BTB domain is also known as BR-C/Ttk or ZiN.


Pssm-ID: 395526 [Multi-domain]  Cd Length: 107  Bit Score: 64.97  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424     67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTD-LIDLQNdglA 140
Cdd:pfam00651    4 LREQGELCDVTLVVGDKEFRAHKAVLAACSPYFkalfsGQESESSVSEITLDDVSPEDFEALLEFMYTGkLISEEN---V 80
                           90       100
                   ....*....|....*....|....*.
gi 62862424    141 LDLLKAAHRFGLPSLLGICERALVTS 166
Cdd:pfam00651   81 DDLLAAADKLQIPSLVDKCEEFLIKS 106
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
1056-1116 1.96e-12

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: 63.13  E-value: 1.96e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62862424 1056 PWAES---DYCQHCTNRFTITMRKHHCRHCGRVLCSKCScndvpilkFGINKPVRVCTVCFNVL 1116
Cdd:cd15716    3 PWVNDsdvPFCPDCGKKFNLARRRHHCRLCGSIMCNKCS--------QFLPLHIRCCHHCKDLL 58
FYVE_PIKfyve_Fab1 cd15725
FYVE domain found in metazoan PIKfyve, fungal and plant Fab1, and similar proteins; PIKfyve, ...
1063-1113 2.23e-12

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: 63.11  E-value: 2.23e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15725   11 CYECSEKFTTFRRRHHCRLCGQIFCSRCCNQEIPGKFIGYPGDLRVCTYCC 61
PHA03100 PHA03100
ankyrin repeat protein; Provisional
528-781 2.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 2.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   528 NKSHDIDFNCQDINgdSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLH-----QSIKNEDSDISLFLLEQGADIT 602
Cdd:PHA03100   23 MEDDLNDYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   603 ALTENLDSALDLSIKHDL--SEVVDALCRRGIALSI-NKNGESPLWSALEKGYED--VAKILVRHGIDTDcwdegpegcr 677
Cdd:PHA03100  101 APDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIkNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN---------- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   678 qtllhraideNKESVAIFLIqSQCDLDSsrqPGPNGEggdeaqdkaSPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKS 757
Cdd:PHA03100  171 ----------AKNRVNYLLS-YGVPINI---KDVYGF---------TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         250       260
                  ....*....|....*....|....*
gi 62862424   758 PLHVAIESQYDEIISILL-CHPDID 781
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLnNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
345-617 4.65e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 MEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDINLRTYdekcaLELSLSMGDHEFLIASILLsmg 424
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTL-----VAIKDAFNNRNVEIFKIIL--- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   425 arTDRTNSKTGDSLLQVFALDRHRGEKSAI---FLADFADLDHIN-FRGLTALHIAALNNMPNLVKKLIVNGASSNLkhI 500
Cdd:PHA02878  122 --TNRYKNIQTIDLVYIDKKSKDDIIEAEItklLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI--P 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   501 DCGLKSALHIAVEANAIDALEAFVElknksHDIDFNCQDINGDSPLSLCLS-LKRTTLVPTLIRGGSDVNGKNK-NNLSP 578
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLE-----NGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYiLGLTA 272
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 62862424   579 LHQSIKNEDsdISLFLLEQGADITALTENLDSALDLSIK 617
Cdd:PHA02878  273 LHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVK 309
FYVE_MTMR4 cd15733
FYVE domain found in myotubularin-related protein 4 (MTMR4) and similar proteins; MTMR4, also ...
1063-1113 5.52e-12

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: 61.68  E-value: 5.52e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15733   10 CFGCDCEFWLAKRKHHCRNCGNVFCADCSNYKLPIPDEQLYDPVRVCNSCY 60
PHA02876 PHA02876
ankyrin repeat protein; Provisional
345-667 6.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 6.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 MEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEFLIASIllsmg 424
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNIDTIKAII----- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   425 arTDRTNSKTGD-SLLQvfALDRHRGEKSAIFLADFADLDHINFRGLTALHIAALN-NMPNLVKKLIVNGASSNLKHIDC 502
Cdd:PHA02876  232 --DNRSNINKNDlSLLK--AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKG 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   503 glKSALHIAVEaNAIDAlEAFVELKNKSHDIdfNCQDINGDSPLSLCLSLKRTT-LVPTLIRGGSDVNGKNKNNLSPLHQ 581
Cdd:PHA02876  308 --ETPLYLMAK-NGYDT-ENIRTLIMLGADV--NAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHY 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   582 SIKNEDSDISLFLLEQGADITALTENLDSALDLSI-KHDLSEVVDALCRRGIAL-SINKNGESPLWSALEKGYE-DVAKI 658
Cdd:PHA02876  382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLIDRGANVnSKNKDLSTPLHYACKKNCKlDVIEM 461

                  ....*....
gi 62862424   659 LVRHGIDTD 667
Cdd:PHA02876  462 LLDNGADVN 470
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
1056-1116 7.15e-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: 61.51  E-value: 7.15e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424 1056 PW---AESDYCQHCTN-RFTITMRKHHCRHCGRVLCSKCSCND--VPILKfgiNKPVRVCTVCFNVL 1116
Cdd:cd15754    1 PWipdKATDICMRCTQtNFSLLTRRHHCRKCGFVVCHECSRQRflIPRLS---PKPVRVCSLCYRKL 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
862-944 1.14e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    862 LHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIqNNADYDATDaDGNNALHIAVRCAQFFIVR 941
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                   ...
gi 62862424    942 ELL 944
Cdd:pfam12796   79 LLL 81
FYVE_FGD1_2_4 cd15741
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein facio-genital dysplasia ...
1059-1116 1.20e-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: 60.96  E-value: 1.20e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424 1059 ESDYCQHCTNRF-TITMRKHHCRHCGRVLCSKCSCNDVPiLKFGINKPVRVCTVCFNVL 1116
Cdd:cd15741    8 EVTMCMRCKEPFnALTRRRHHCRACGYVVCWKCSDYKAT-LEYDGNKLNRVCKHCYVIL 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
456-667 1.26e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   456 LADFADLDHINFRGLTALHIAALNNMPNL---VKKLIVNGASSNLKHIdCGLkSALHIAVE-ANAIDALEAFVElknksH 531
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPER-CGF-TPLHLYLYnATTLDVIKLLIK-----A 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   532 DIDFNCQDINGDSPLSLCLSLKRT--TLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISL--FLLEQGADITALTEN 607
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELlrLLIDAGADVYAVDDR 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424   608 LDSALD---LSIKHDlSEVVDALCRRGI-ALSINKNGESPLWSALEKGYEDVAKI--LVRHGIDTD 667
Cdd:PHA03095  187 FRSLLHhhlQSFKPR-ARIVRELIRAGCdPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISIN 251
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
1052-1117 1.35e-11

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: 61.10  E-value: 1.35e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424 1052 PQESPWAESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPiLKFGINKPVRVCTVCFNVLQ 1117
Cdd:cd15742    1 PTLVPVSHVMMCMNCGSDFTLTLRRHHCHACGKIVCRNCSRNKYP-LKYLKDRPAKVCDGCFAELR 65
PHA02874 PHA02874
ankyrin repeat protein; Provisional
484-764 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   484 LVKKLIVNGASSNlkHIDCGLKSALHIAVEANAIDALEAFVelknkshdidfncqdINGDSPLSLCLSLKRTTLVPTLIR 563
Cdd:PHA02874   50 IVELFIKHGADIN--HINTKIPHPLLTAIKIGAHDIIKLLI---------------DNGVDTSILPIPCIEKDMIKTILD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   564 GGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINK-NGES 642
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDnNGES 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   643 PLWSALEKGYEDVAKILVRHG--IDTDCwDEGpegcrQTLLHRAIDENKESVAIFLiqsqcdldssrqpgPNGEGGDEAQ 720
Cdd:PHA02874  193 PLHNAAEYGDYACIKLLIDHGnhIMNKC-KNG-----FTPLHNAIIHNRSAIELLI--------------NNASINDQDI 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 62862424   721 DKASPLHLCCHWGQTK-VLQTLIDHGANVNLIDAESKSPLHVAIE 764
Cdd:PHA02874  253 DGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTAFK 297
FYVE_ZFYV1 cd15734
FYVE domains found in zinc finger FYVE domain-containing protein 1 (ZFYV1) and similar ...
1063-1113 1.69e-11

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: 60.42  E-value: 1.69e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15734   11 CSVCKRPFSPRLSKHHCRACGQGVCDDCSKNRRPVPSRGWDHPVRVCDPCA 61
Ank_2 pfam12796
Ankyrin repeats (3 copies);
827-921 2.34e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    827 LHLAILKDDLESVLFLLAIQVDVNsrVHDANQSSPLHLAAASQNEMITRnLILAGARMNERDAvQKLPLHIAIERGNLPA 906
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 62862424    907 VSALIQNNADYDATD 921
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
FYVE_MTMR3 cd15732
FYVE domain found in myotubularin-related protein 3 (MTMR3) and similar proteins; MTMR3, also ...
1063-1113 2.78e-11

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: 59.91  E-value: 2.78e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15732   11 CYGCEREFWLASRKHHCRNCGNVFCGSCCNQKLPVPSQQLFEPSRVCKSCF 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
561-900 2.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   561 LIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRgiALSINKNG 640
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN--RSNINKND 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   641 ESpLWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDENKESVAI-FLIQSQCDLDSSRQPGpngeggdea 719
Cdd:PHA02876  242 LS-LLKAIRNEDLETSLLLYDAGFSVNSIDD----CKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKG--------- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   720 qdkASPLHLCCHWG-QTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALd 798
Cdd:PHA02876  308 ---ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAA- 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   799 FRNHNAAQRILDRFPTAAEQMDIRGRNFLHLAIL-KDDLESVLFLLAIQVDVNSRVHDAnqSSPLHLAAASQNEM-ITRN 876
Cdd:PHA02876  384 VRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDL--STPLHYACKKNCKLdVIEM 461
                         330       340
                  ....*....|....*....|....
gi 62862424   877 LILAGARMNERDAVQKLPLHIAIE 900
Cdd:PHA02876  462 LLDNGADVNAINIQNQYPLLIALE 485
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
840-1030 4.15e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  840 LFLLAIQVDVNSRVHDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDA 919
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  920 TDADGNNALHIAVRCAQFFIVRELLtESRVNAEATNLKGRNPLHELCRvvEDSTAglICELFLESmpKYPINIPDMDGNT 999
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAY--NGNLE--IVKLLLEA--GADVNAQDNDGNT 155
                        170       180       190
                 ....*....|....*....|....*....|.
gi 62862424 1000 PLLLSFMRGQSPLCKILVKAGACLGTENKDG 1030
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
Ank_2 pfam12796
Ankyrin repeats (3 copies);
895-963 4.50e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 4.50e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424    895 LHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLTESRVNAeatNLKGRNPLH 963
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALH 66
Ank_2 pfam12796
Ankyrin repeats (3 copies);
726-811 6.58e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 6.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    726 LHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIDLKLrdkSGNTPFATALDFRNHNAA 805
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIV 77

                   ....*.
gi 62862424    806 QRILDR 811
Cdd:pfam12796   78 KLLLEK 83
PHA02874 PHA02874
ankyrin repeat protein; Provisional
546-990 6.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   546 LSLCLSLKRTTLVPTLIRG-GSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITaltenldsaldlsikhdlsevv 624
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADIN---------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   625 dalcrrgialSINKNGESPLWSALEKGYEDVAKILVRHGIDTDCWdegPEGCRqtllhraideNKESVAIFLiqsQCDLD 704
Cdd:PHA02874   63 ----------HINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL---PIPCI----------EKDMIKTIL---DCGID 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   705 SSRQpgpngeggdEAQDKaSPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLcHPDIDLKL 784
Cdd:PHA02874  117 VNIK---------DAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANV 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   785 RDKSGNTPFATALDFRNHNAAQRILDRFPTAAEQMDiRGRNFLHLAILKDdlESVLFLLAIQVDVNsrVHDANQSSPLHL 864
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN--RSAIELLINNASIN--DQDIDGSTPLHH 260
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   865 AAasqnemitrnlilagarmnerdavqKLPLHIAIergnlpaVSALIQNNADYDATDADGNNALHIAVR-CAQFFIVREL 943
Cdd:PHA02874  261 AI-------------------------NPPCDIDI-------IDILLYHKADISIKDNKGENPIDTAFKyINKDPVIKDI 308
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 62862424   944 LTESRVNAEATNLKGRNPLHELCRVVEDSTAGLI--CELFLESMPKYPI 990
Cdd:PHA02874  309 IANAVLIKEADKLKDSDFLEHIEIKDNKEFSDFIkeCNEEIEDMKKTKC 357
PHA03100 PHA03100
ankyrin repeat protein; Provisional
243-392 7.53e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   243 IQKYGnSLVNTFSENGILPLEMALSSK--NAKIAKSLVDNGmANINAVNMEGFSLLKSALKNG--DAFSANFLLDQ---- 314
Cdd:PHA03100   92 LLEYG-ANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKgvdi 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   315 ------NCLLDLPSKPSS-----DTALHIICNYgpdNTPEImevVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKL 383
Cdd:PHA03100  170 naknrvNYLLSYGVPINIkdvygFTPLHYAVYN---NNPEF---VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243
                         170
                  ....*....|
gi 62862424   384 LLKV-PNIDI 392
Cdd:PHA03100  244 LLNNgPSIKT 253
BTB2_POZ_RhoBTB cd18300
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
66-167 8.29e-11

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, a tandem of 2 BTB domains, and a conserved C-terminal region. In humans, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349609 [Multi-domain]  Cd Length: 108  Bit Score: 59.95  E-value: 8.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   66 SLFDKNTYADIYIRSQTRVFPAHKIVLHARSEkW------GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGL 139
Cdd:cd18300    2 LFLNKGLFSDVTFIVEDGTIPAHKALLVARCD-VmaamfgGNFRESSAKEVELPGVSKETFLALLEYLYTDQAPILEDGD 80
                         90       100
                 ....*....|....*....|....*...
gi 62862424  140 ALDLLKAAHRFGLPSLLGICERALVTSV 167
Cdd:cd18300   81 CVGLIVLANRLCLPRLVALCEQYIVKEL 108
Ank_2 pfam12796
Ankyrin repeats (3 copies);
330-431 1.20e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    330 LHIICNYGPdntpeiMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDInlrTYDEKCALELSLSM 409
Cdd:pfam12796    1 LHLAAKNGN------LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARS 71
                           90       100
                   ....*....|....*....|..
gi 62862424    410 GDHEflIASILLSMGARTDRTN 431
Cdd:pfam12796   72 GHLE--IVKLLLEKGADINVKD 91
BTB_POZ_ZBTB_KLHL-like cd18186
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
73-150 1.38e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing (ZBTB) proteins, Kelch-like (KLHL) proteins, and similar proteins; This family includes a variety of BTB/POZ domain-containing proteins, such as zinc finger and BTB domain-containing (ZBTB) proteins and Kelch-like (KLHL) proteins. They have diverse functions, such as transcriptional regulation, chromatin remodeling, protein degradation and cytoskeletal regulation. Many BTB/POZ proteins contain one or two additional domains, such as kelch repeats, zinc-finger domains, FYVE (Fab1, YOTB, Vac1, and EEA1) fingers, or ankyrin repeats. These special additional domains or interaction partners provide unique characteristics and functions to BTB/POZ proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349497 [Multi-domain]  Cd Length: 82  Bit Score: 58.33  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   73 YADIYIRSQTRVFPAHKIVLHARSEK-----WGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLqNDGLALDLLKAA 147
Cdd:cd18186    1 LCDVTLVVGGREFPAHRAVLAARSPYframfSSGMKESSSSEIELDDVSPEAFEALLDYIYTGELEL-SEENVEELLAAA 79

                 ...
gi 62862424  148 HRF 150
Cdd:cd18186   80 DKL 82
FYVE_PKHF2 cd15755
FYVE domain found in protein containing both PH and FYVE domains 2 (phafin-2) and similar ...
1056-1116 1.40e-10

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: 58.12  E-value: 1.40e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424 1056 PWAESDYCQHCTN-RFTITMRKHHCRHCGRVLCSKCSCNDVpILKFGINKPVRVCTVCFNVL 1116
Cdd:cd15755    4 PDSEATVCMRCQKaKFTPVNRRHHCRKCGFVVCGPCSEKKF-LLPSQSSKPVRVCDFCYDLL 64
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
1057-1114 1.93e-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: 57.53  E-value: 1.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424 1057 WAESDYCQHC----TNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINkPVRVCTVCFN 1114
Cdd:cd15724    1 WVPDEAVSVCmvcqVERFSMFNRRHHCRRCGRVVCSSCSTKKMLVEGYREN-PVRVCDQCYE 61
BTB_POZ_BTBD9 cd18287
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-155 2.52e-10

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 9 (BTBD9); BTBD9 is a risk factor for Restless Legs Syndrome (RLS) encoding a Cullin-3 substrate adaptor. The BTBD9 gene may be associated with antipsychotic-induced RLS in schizophrenia. Mutations in BTBD9 lead to reduced dopamine, increased locomotion and sleep fragmentation. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349596 [Multi-domain]  Cd Length: 119  Bit Score: 59.17  E-value: 2.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEK-----WGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQN-- 136
Cdd:cd18287   13 IGALFLNEEYSDVTFVVEEKRFPAHRVILAARSEYfrallYGGMRESQQSEIELKDTNAEAFKALLKYIYTGRLTLTDlk 92
                         90
                 ....*....|....*....
gi 62862424  137 DGLALDLLKAAHRFGLPSL 155
Cdd:cd18287   93 EDVLLDVLGLAHQYGFEEL 111
FYVE_RUFY2 cd15759
FYVE domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
1059-1116 2.75e-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: 57.34  E-value: 2.75e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62862424 1059 ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILkfGINKPVRVCTVCFNVL 1116
Cdd:cd15759    9 EATHCKLCEKEFSLSKRKHHCRNCGEIFCNACSDNELPLP--SSPKPVRVCDSCHAML 64
PHA02875 PHA02875
ankyrin repeat protein; Provisional
345-639 3.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 MEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVPNIDiNLRTYDEKCALELSLSMGDhefliasillsmg 424
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGD------------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   425 artdrtnSKTGDSLLQvfaldrhrgeksaifLADFADlDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHIDcgL 504
Cdd:PHA02875   81 -------VKAVEELLD---------------LGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD--K 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   505 KSALHIAVEANAIDALEAFVElknksHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKN-NLSPLHQSI 583
Cdd:PHA02875  136 FSPLHLAVMMGDIKGIELLID-----HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAI 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424   584 KNEDSDISLFLLEQGAD---ITALTENLDSALDLSIKHDL---SEVVDALCRRgIALSINKN 639
Cdd:PHA02875  211 ENNKIDIVRLFIKRGADcniMFMIEGEECTILDMICNMCTnleSEAIDALIAD-IAIRIHKK 271
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
1063-1113 3.48e-10

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: 56.36  E-value: 3.48e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15745    2 CAICAKAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVPDTCIYLRVCKTCY 52
PHA02874 PHA02874
ankyrin repeat protein; Provisional
345-690 1.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 MEVVKKILQRQLN-INIQNIKGETPLHIAIARRNVEMVKLLLKvPNIDINLRTYDEKCALELSLSMGDHEflIASILLSM 423
Cdd:PHA02874   14 IEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIK-HGADINHINTKIPHPLLTAIKIGAHD--IIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   424 GARTdrtnsktgdSLLQVFALDRhrgEKSAIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHIDCG 503
Cdd:PHA02874   91 GVDT---------SILPIPCIEK---DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGC 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   504 LksALHIAVEANAIDALEAFVElkNKSHdidFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSI 583
Cdd:PHA02874  159 Y--PIHIAIKHNFFDIIKLLLE--KGAY---ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   584 KNEDSDISLFLleQGADITALTENLDSALDLSIKHDLS-EVVDALCRRGIALSI-NKNGESPLWSALEKGYED-VAKILV 660
Cdd:PHA02874  232 IHNRSAIELLI--NNASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIkDNKGENPIDTAFKYINKDpVIKDII 309
                         330       340       350
                  ....*....|....*....|....*....|
gi 62862424   661 RHGIDTDCWDEGPEGcrQTLLHRAIDENKE 690
Cdd:PHA02874  310 ANAVLIKEADKLKDS--DFLEHIEIKDNKE 337
FYVE_WDFY2 cd15757
FYVE domain found in WD40 repeat and FYVE domain-containing protein 2 (WDFY2); WDFY2, also ...
1057-1112 1.27e-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: 55.46  E-value: 1.27e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424 1057 WAESDYCQHCTNRF-----------TITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVC 1112
Cdd:cd15757    3 WLDSDSCQKCDQPFfwnfkqmwdskKIGLRQHHCRKCGKAVCGKCSSKRSTIPLMGFEFEVRVCDSC 69
Ank_2 pfam12796
Ankyrin repeats (3 copies);
579-665 1.29e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    579 LHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRgIALSINKNGESPLWSALEKGYEDVAKI 658
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                   ....*..
gi 62862424    659 LVRHGID 665
Cdd:pfam12796   80 LLEKGAD 86
BTB_POZ_ABTB2-like cd18297
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-169 1.35e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 2 (ABTB2) and similar proteins; This family includes ABTB2, BTBD11, plant ARM repeat protein interacting with ABF2 (ARIA), and similar proteins. ABTB2, also called bood POZ containing gene type 2 (BPOZ-2), is a scaffold protein that controls the degradation of many biological proteins ranging from embryonic development to tumor progression. It may be involved in the initiation of hepatocyte growth. ABTB2 functions as an adaptor protein for the E3 ubiquitin ligase scaffold protein Cullin-3. It directly binds to eukaryotic elongation factor 1A1 (eEF1A1) to promote eEF1A1 ubiquitylation and degradation, and prevent translation. The BTBD11 gene has been recently identified as an all-trans retinoic acid (atRA)-responsive gene that lies downstream of atRA and its receptors in the regulation of neurite outgrowth and cell adhesion in neural as well as non-neural tissues. ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349606 [Multi-domain]  Cd Length: 117  Bit Score: 56.90  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQ-----QLDWSDLNEDVVLSLLRWIYTDLIDLQNDGL-- 139
Cdd:cd18297    6 YVNNPEMSDVTFLVEGRPFYAHKIVLVTASDRFKSMLSSGSTeaqtpVIEIPDIRYDIFQLMMQYLYTGGVESLDVAQdd 85
                         90       100       110
                 ....*....|....*....|....*....|
gi 62862424  140 ALDLLKAAHRFGLPSLLGICERALVTSVGV 169
Cdd:cd18297   86 ALELLRAASFFQLDGLKRHCEILLSQQIDL 115
PHA02875 PHA02875
ankyrin repeat protein; Provisional
265-497 1.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   265 ALSSKNAKIAKSLVDNGMaNINAVNMEGFSLLKSALKNGDAFSANFLLDQNCLLDLpSKPSSDTALHIICNYGpdntpei 344
Cdd:PHA02875    9 AILFGELDIARRLLDIGI-NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV-KYPDIESELHDAVEEG------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 mEVVKKILQRQLNINIQNI---KGETPLHIAIARRNVEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEFLiaSILL 421
Cdd:PHA02875   80 -DVKAVEELLDLGKFADDVfykDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGI--ELLI 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424   422 SMGARTDRTNSKTGDSLLqvFALDRHRGEKSAIFLADFADLDHINFRG-LTALHIAALNNMPNLVKKLIVNGASSNL 497
Cdd:PHA02875  156 DHKACLDIEDCCGCTPLI--IAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
FYVE2_Vac1p_like cd15737
FYVE domain 2 found in yeast protein VAC1 (Vac1p) and similar proteins; Vac1p, also termed ...
1056-1112 1.73e-09

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: 55.59  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424 1056 PWaESD----YCQHCTNRFTITMRKHHCRHCGRVLCS----KCScNDVPI---------LKFGINKP----------VRV 1108
Cdd:cd15737    1 PW-EDDssvtHCPICLRSFGLLLRKHHCRLCGKVVCDdrrtKCS-TEVPLdllssalpdLPFVFKEPqsdipddtksVRV 78

                 ....
gi 62862424 1109 CTVC 1112
Cdd:cd15737   79 CRDC 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
243-601 2.77e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   243 IQKYGNSLvNTFSENGILPLEMALSSKNAKIAKSLVDNGmANINAVNMEGFSLLKSALKNGDAFSANFLLDQNClldlps 322
Cdd:PHA02874   21 IKNKGNCI-NISVDETTTPLIDAIRSGDAKIVELFIKHG-ADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV------ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   323 kpssDTALHIIcnygpdntPEI-MEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVpNIDINLRtyDEKC 401
Cdd:PHA02874   93 ----DTSILPI--------PCIeKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIE--DDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   402 ALELSLSMGDHEFLIASILLSMGARTDrTNSKTGDSLLQVFAldrHRGEKSAIFLAdfadLDHINF------RGLTALHI 475
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAA---EYGDYACIKLL----IDHGNHimnkckNGFTPLHN 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   476 AALNNMPnlVKKLIVNGASSNLKHID--CGLKSALHIAVEANAIDALeafveLKNKShdiDFNCQDINGDSPLSLCLS-L 552
Cdd:PHA02874  230 AIIHNRS--AIELLINNASINDQDIDgsTPLHHAINPPCDIDIIDIL-----LYHKA---DISIKDNKGENPIDTAFKyI 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 62862424   553 KRTTLVPTLIRGGSDVN--GKNKNNLSPLHQSIKnEDSDISLFLLEQGADI 601
Cdd:PHA02874  300 NKDPVIKDIIANAVLIKeaDKLKDSDFLEHIEIK-DNKEFSDFIKECNEEI 349
PHA02875 PHA02875
ankyrin repeat protein; Provisional
830-1021 3.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   830 AILKDDLESVLFLLAIQVDVNSRVHDAnqSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSA 909
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDG--ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   910 LIQNN--ADyDATDADGNNALHIAVRCAQFFIVReLLTESRVNAEATNLKGRNPLHeLCRVVEDSTAgliCELFLESmpK 987
Cdd:PHA02875   87 LLDLGkfAD-DVFYKDGMTPLHLATILKKLDIMK-LLIARGADPDIPNTDKFSPLH-LAVMMGDIKG---IELLIDH--K 158
                         170       180       190
                  ....*....|....*....|....*....|....
gi 62862424   988 YPINIPDMDGNTPLLLSFMRGQSPLCKILVKAGA 1021
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA03100 PHA03100
ankyrin repeat protein; Provisional
827-1031 3.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.45  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   827 LHLAILKDDLESVLFLLAIQVDVNSrvHDANQSSPLHLAAasqNEM--ITRN------LILAGARMNERDAVQKLPLHIA 898
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINS--STKNNSTPLHYLS---NIKynLTDVkeivklLLEYGANVNAPDNNGITPLLYA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   899 I--ERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQF-FIVRELLTESRVNAEATNlkgrnplhelcRVvedstag 975
Cdd:PHA03100  114 IskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdLKILKLLIDKGVDINAKN-----------RV------- 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424   976 licELFLESmpKYPINIPDMDGNTPLLLSFMRGQSPLCKILVKAGACLGTENKDGI 1031
Cdd:PHA03100  176 ---NYLLSY--GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
BTB_POZ_KLHL40_KBTBD5 cd18340
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-173 6.37e-09

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 40 (KLHL40); KLHL40, also called Kelch repeat and BTB domain-containing protein 5 (KBTBD5) or sarcosynapsin, is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. Mutations in KLHL40 may cause severe autosomal-recessive nemaline myopathy. KLHL40 contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349649 [Multi-domain]  Cd Length: 134  Bit Score: 55.61  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQ-----QLDWSDLNEDVVLSLLRWIYTDLIDLqNDGLAL 141
Cdd:cd18340   21 LLDHNKFVDCVLKIKEKEFPCHRLVLAACSPYFRAMFLSDLEeskkrEIVLEDVDPDVMGKILHYIYTSEIEI-TEQNVQ 99
                         90       100       110
                 ....*....|....*....|....*....|..
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCI 173
Cdd:cd18340  100 DIFAAANMFQIPSIFTVCVSFLQKRLCLSNCL 131
BTB_POZ_roadkill-like cd18345
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
66-169 1.01e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Drosophila melanogaster protein roadkill and similar proteins; Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349654 [Multi-domain]  Cd Length: 121  Bit Score: 54.47  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   66 SLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQ-----LDWSDLNEDVVLSLLRWIYTDLIDlQNDGLA 140
Cdd:cd18345   11 LLFERSAFSDVTLCVGGREFQAHKAILAARSPVFNAMFEHEMEErkqnrVEITDVDHEVMREMLRFIYTGKAP-NLDKMA 89
                         90       100
                 ....*....|....*....|....*....
gi 62862424  141 LDLLKAAHRFGLPSLLGICERALVTSVGV 169
Cdd:cd18345   90 DDLLAAADKYALERLKVMCEEALCSNLSV 118
Ank_2 pfam12796
Ankyrin repeats (3 copies);
473-572 1.08e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    473 LHIAALNNMPNLVKKLIVNGASSNLKhiDCGLKSALHIAVEANAIDALEAFVELknkshdIDFNCQDiNGDSPLSLCLSL 552
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQ--DKNGRTALHLAAKNGHLEIVKLLLEH------ADVNLKD-NGRTALHYAARS 71
                           90       100
                   ....*....|....*....|
gi 62862424    553 KRTTLVPTLIRGGSDVNGKN 572
Cdd:pfam12796   72 GHLEIVKLLLEKGADINVKD 91
FYVE_FYCO1 cd15726
FYVE domain found in FYVE and coiled-coil domain-containing protein 1 (FYCO1) and similar ...
1059-1113 1.10e-08

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: 52.56  E-value: 1.10e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424 1059 ESDYCQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGinKPVRVCTVCF 1113
Cdd:cd15726    6 DVTHCLDCKSEFSWMVRRHHCRLCGRIFCYACSNFYVLTAHGG--KKERCCKACF 58
BTB smart00225
Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. ...
75-166 1.45e-08

Broad-Complex, Tramtrack and Bric a brac; Domain in Broad-Complex, Tramtrack and Bric a brac. Also known as POZ (poxvirus and zinc finger) domain. Known to be a protein-protein interaction motif found at the N-termini of several C2H2-type transcription factors as well as Shaw-type potassium channels. Known structure reveals a tightly intertwined dimer formed via interactions between N-terminal strand and helix structures. However in a subset of BTB/POZ domains, these two secondary structures appear to be missing. Be aware SMART predicts BTB/POZ domains without the beta1- and alpha1-secondary structures.


Pssm-ID: 197585 [Multi-domain]  Cd Length: 97  Bit Score: 53.46  E-value: 1.45e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424      75 DIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQLDWS-----DLNEDVVLSLLRWIYTDLIDLqNDGLALDLLKAAHR 149
Cdd:smart00225    1 DVTLVVGGKKFHAHKAVLAAHSPYFKALFSSDFKESDKSeiyldDVSPEDFRALLNFLYTGKLDL-PEENVEELLELADY 79
                            90
                    ....*....|....*..
gi 62862424     150 FGLPSLLGICERALVTS 166
Cdd:smart00225   80 LQIPGLVELCEEFLLKL 96
PHA03095 PHA03095
ankyrin-like protein; Provisional
345-630 1.79e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   345 MEVVKKILQRQLNINIQNIKGETPLHIAIARRN---VEMVKLLLKVpNIDINLRTYDEKCALELSLSMGDHEFLIAsILL 421
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEA-GADVNAPERCGFTPLHLYLYNATTLDVIK-LLI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   422 SMGARTDRTNsKTGDSLLQVFALDRHRGEKSAIFLADF-ADLDHINFRGLTALHIAALNN--MPNLVKKLIvnGASSNLK 498
Cdd:PHA03095  105 KAGADVNAKD-KVGRTPLHVYLSGFNINPKVIRLLLRKgADVNALDLYGMTPLAVLLKSRnaNVELLRLLI--DAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   499 HIDCGLKSALHIavEANAIDALEAFVElKNKSHDIDFNCQDINGDSPLSLCL---SLKRTTLVPtLIRGGSDVNGKNKNN 575
Cdd:PHA03095  182 AVDDRFRSLLHH--HLQSFKPRARIVR-ELIRAGCDPAATDMLGNTPLHSMAtgsSCKRSLVLP-LLIAGISINARNRYG 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424   576 LSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRR 630
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
BTB_POZ_BTBD19 cd18294
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
65-161 2.06e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 19 (BTBD19); BTBD19 is a BTB domain-containing protein. Its function remains unclear. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349603 [Multi-domain]  Cd Length: 111  Bit Score: 53.40  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   65 ASLFDKNTYADI-YIRSQTR-VFPAHKIVLHARSEKWGNDLLSNIQQ------LDWSDLNEDVVLSLLRWIYTDLIDLQN 136
Cdd:cd18294    6 KSLINNPEFSDVkFLVGPERqEIFAHKCILAARCEVFRAMFLTGPQKestqspLVLSDIEPEVFRAVLEFIYTNCVTLSN 85
                         90       100
                 ....*....|....*....|....*
gi 62862424  137 DgLALDLLKAAHRFGLPSLLGICER 161
Cdd:cd18294   86 H-TVIEVLAAAVEYGLDELRKLCER 109
BTB_POZ_KLHL40-like cd18269
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-173 3.74e-08

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins, KLHL40 and KLHL41; This family includes Kelch-like proteins, KLHL40 and KLHL41. KLHL40 is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a key regulator of skeletal muscle development. KLHL41 is a novel kelch related protein that is involved in pseudopod elongation in transformed cells. They both contain a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349578 [Multi-domain]  Cd Length: 133  Bit Score: 53.18  E-value: 3.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQ-----QLDWSDLNEDVVLSLLRWIYTDLIDLqNDGLAL 141
Cdd:cd18269   21 LLDENKFVDCVLKIGDKEFPCHRLVLAACSPYFRAMFLSDLEeskkkEVVLEDVDPDVMGMILKYLYTSEIDL-NDQNVQ 99
                         90       100       110
                 ....*....|....*....|....*....|..
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCI 173
Cdd:cd18269  100 DIFALASRFQIPSIFTVCVSYLQKRLSLSNCL 131
Ank_4 pfam13637
Ankyrin repeats (many copies);
894-944 5.61e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 5.61e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 62862424    894 PLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELL 944
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
702-882 7.05e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   702 DLDSSRQPGPNGEGGDEAQDKASPLHLCCHwGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPdID 781
Cdd:PLN03192  506 DLNVGDLLGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   782 LKLRDKSGNTPFATALDfRNHNAAQRILDRFPTAAEQMdiRGRNFLHLAILKDDLESVLFLLAIQVDVNSRVHDAnqSSP 861
Cdd:PLN03192  584 VHIRDANGNTALWNAIS-AKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQG--ATA 658
                         170       180
                  ....*....|....*....|.
gi 62862424   862 LHLAAASQNEMITRNLILAGA 882
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGA 679
BTB2_POZ_ABTB1_BPOZ1 cd18296
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
69-163 8.45e-08

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349605 [Multi-domain]  Cd Length: 121  Bit Score: 51.91  E-value: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   69 DKNTYADIYIRSQTRVFPAHKIVLHARSEKWgNDLL-----------SNIQQLDWSDLNEDVVLSLLRWIYTDLIDLqND 137
Cdd:cd18296   13 QELSFPDVCFQVEGHRFPCHKAFFCGRSDYF-KALLrdhfaeseennGSIPVVTLHDVSPEVFAIVLYYIYTDDTDL-PP 90
                         90       100
                 ....*....|....*....|....*.
gi 62862424  138 GLALDLLKAAHRFGLPSLLGICERAL 163
Cdd:cd18296   91 ENAYDVLYVADMYLLPGLKRLCGTVL 116
Ank_2 pfam12796
Ankyrin repeats (3 copies);
508-603 9.16e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 9.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    508 LHIAVEANAIDALEAFVElknksHDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRGGsDVNGKNkNNLSPLHQSIKNED 587
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-----NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGH 73
                           90
                   ....*....|....*.
gi 62862424    588 SDISLFLLEQGADITA 603
Cdd:pfam12796   74 LEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
644-752 1.08e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    644 LWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDENKESVAIFLIqsqcdldssrqpgpNGEGGDEAQDKA 723
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK----NGRTALHLAAKNGHLEIVKLLL--------------EHADVNLKDNGR 62
                           90       100
                   ....*....|....*....|....*....
gi 62862424    724 SPLHLCCHWGQTKVLQTLIDHGANVNLID 752
Cdd:pfam12796   63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
FYVE_FGD3 cd15740
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 3 (FGD3) and similar ...
1059-1113 1.12e-07

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: 49.61  E-value: 1.12e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424 1059 ESDYCQHCTNRF-TITMRKHHCRHCGRVLCSKCScndvpILKFGINKPVRVCTVCF 1113
Cdd:cd15740    4 EKQTCKGCNESFnSITKRRHHCKQCGAVICGKCS-----EFKDLASRHNRVCRDCF 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
679-916 1.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   679 TLLHRAIDENKESVAIFLIQSQCDLDSSrqpgpngeggdeAQDKASPLHLCCHWG--QTKVLQT---LIDHGANVNLIDA 753
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSS------------TKNNSTPLHYLSNIKynLTDVKEIvklLLEYGANVNAPDN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   754 ESKSPLHVAI--ESQYDEIISILLCHpDIDLKLRDKSGNTPFATALD--FRNHNAAQRILDRfptaaeQMDIRGRNflhl 829
Cdd:PHA03100  105 NGITPLLYAIskKSNSYSIVEYLLDN-GANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDK------GVDINAKN---- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   830 ailkddleSVLFLLAIQVDVNSRvhDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSA 909
Cdd:PHA03100  174 --------RVNYLLSYGVPINIK--DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                  ....*..
gi 62862424   910 LIQNNAD 916
Cdd:PHA03100  244 LLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
328-385 1.45e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.45e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 62862424    328 TALHIICNYGPdntpeiMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLL 385
Cdd:pfam13637    3 TALHAAAASGH------LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
FYVE_scVPS27p_Vac1p_like cd15736
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
1063-1113 1.92e-07

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: 48.72  E-value: 1.92e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPI----LKFGINKPVRVCTVCF 1113
Cdd:cd15736    2 CHTCSRTFNLNIRAHHCRKCGKLFCRRHLPNMIPLnlsaYDPRNGKWYRCCHSCF 56
BTB_POZ_SPOP-like cd18279
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-171 3.86e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP) and similar proteins; This family includes speckle-type POZ protein (SPOP), speckle-type POZ protein-like (SPOPL), TD and POZ domain-containing proteins (TDPOZ), Drosophila melanogaster protein roadkill and similar proteins. Both, SPOP and SPOPL, serve as adaptors of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and proteasomal degradation of target proteins. TDPOZ is a family of bipartite animal and plant proteins that contain a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domains. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. Drosophila melanogaster protein roadkill, also called Hh-induced MATH and BTB domain-containing protein (HIB), is a hedgehog-induced BTB protein that modulates hedgehog signaling by degrading Ci/Gli transcription factor. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349588 [Multi-domain]  Cd Length: 120  Bit Score: 49.84  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWgNDLL------SNIQQLDWSDLNEDVVLSLLRWIYTDLIDlQNDGLA 140
Cdd:cd18279   12 LWENSRFTDCCLCVGGQEFQAHKAILAARSPVF-SAMFehemeeSKKNRVEINDVDPEVFKEMMRFIYTGKAP-NLDKMA 89
                         90       100       110
                 ....*....|....*....|....*....|.
gi 62862424  141 LDLLKAAHRFGLPSLLGICERALVTSVGVRS 171
Cdd:cd18279   90 DDLLAAADKYALERLKVMCEDALCSNLSVEN 120
PHA02875 PHA02875
ankyrin repeat protein; Provisional
733-945 6.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   733 GQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDI-DLKLRDKsgNTPFATALDFRNHNAAQRILDR 811
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDI--ESELHDAVEEGDVKAVEELLDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   812 FPTAAEQMDIRGRNFLHLAILKDDLESVLFLLAIQVDVNsrVHDANQSSPLHLAAASQNEMITRNLILAGARMNERDAVQ 891
Cdd:PHA02875   91 GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD--IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424   892 KLPLHIAIERGNLPAVSALIQNNADYDATDADGN-NALHIAVRCAQFFIVRELLT 945
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
226-497 6.18e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   226 PLHAAVRL---LREDVVSLCIQKYGNslVNTFSENGILPLEMALSSKN-AKIAKSLVDNGmANINAVNMEGFSLLKSALK 301
Cdd:PHA03095   50 PLHLYLHYsseKVKDIVRLLLEAGAD--VNAPERCGFTPLHLYLYNATtLDVIKLLIKAG-ADVNAKDKVGRTPLHVYLS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   302 NgdaFSANFlldqnclldlpskpssdtalhiicnygpdntpeimEVVKKILQRQLNINIQNIKGETPLHIAIARRN--VE 379
Cdd:PHA03095  127 G---FNINP-----------------------------------KVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   380 MVKLLLK----VPNIDINLRTydekcALelslsmgdHEFL--------IASILLSMGARTDRTNSKTGDSLLQVFALDRH 447
Cdd:PHA03095  169 LLRLLIDagadVYAVDDRFRS-----LL--------HHHLqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSSC 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 62862424   448 RGEKSAIFLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNL 497
Cdd:PHA03095  236 KRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285
FYVE_RUFY3 cd15744
FYVE-related domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar ...
1063-1113 6.82e-07

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: 47.03  E-value: 6.82e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62862424 1063 CQHC-TNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINkPVRVCTVCF 1113
Cdd:cd15744    2 CSLCqEDFASLALPKHNCYNCGGTFCDACSSNELPLPSSIYE-PARVCDVCY 52
BTB_POZ_KLHL41_KBTBD10 cd18341
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
67-173 8.64e-07

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 41 (KLHL41); KLHL41 is also called Kel-like protein 23, Kelch repeat and BTB domain-containing protein 10 (KBTBD10), Kelch-related protein 1 (Krp1), or sarcosine. It is a novel kelch-related protein that is involved in pseudopod elongation in transformed cells. It is also involved in skeletal muscle development and differentiation. It regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349650 [Multi-domain]  Cd Length: 133  Bit Score: 49.46  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNI-----QQLDWSDLNEDVVLSLLRWIYTDLIDLqNDGLAL 141
Cdd:cd18341   21 LLDENKFVDCTLKAGDKSLPCHRLILAACSPYFREYFLSEEseekkKEVVLDNVDPNIMDMILKYLYSAEIDL-NDGNVQ 99
                         90       100       110
                 ....*....|....*....|....*....|..
gi 62862424  142 DLLKAAHRFGLPSLLGICERALVTSVGVRSCI 173
Cdd:cd18341  100 DIFALASRFQIPSVFTVCVTYLQKRLSPANCL 131
PHA02875 PHA02875
ankyrin repeat protein; Provisional
789-972 8.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   789 GNTPFATALDFRNhNAAQRILDRFPTAAEQMDIRGRNFLHLAILKDDLESVLFLLaiqvDVNSRVHDA---NQSSPLHLA 865
Cdd:PHA02875   35 GISPIKLAMKFRD-SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL----DLGKFADDVfykDGMTPLHLA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   866 AASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLt 945
Cdd:PHA02875  110 TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL- 188
                         170       180
                  ....*....|....*....|....*...
gi 62862424   946 ESRVNaeaTNLKGRNP-LHELCRVVEDS 972
Cdd:PHA02875  189 DSGAN---IDYFGKNGcVAALCYAIENN 213
PHA02878 PHA02878
ankyrin repeat protein; Provisional
339-670 9.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   339 DNTPEIMEVVKKILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKVpniDINLRTYDEKCALELSLSMGDHEFLIAS 418
Cdd:PHA02878   11 DNYETILKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTR---GHNVNQPDHRDLTPLHIICKEPNKLGMK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   419 ILLSmgartdrtnSKTGDSLlqvfaldrhrgeksaifladfadldhinFRGLTALHIAALNNMPNLVKKLIVNGA----S 494
Cdd:PHA02878   88 EMIR---------SINKCSV----------------------------FYTLVAIKDAFNNRNVEIFKIILTNRYkniqT 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   495 SNLKHIDcglksalhiavEANAIDALEAFVELKNKSHDIDFNCQDIN-GDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNK 573
Cdd:PHA02878  131 IDLVYID-----------KKSKDDIIEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   574 NNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLS-EVVDALCRRGIALSINKN--GESPLWSALEK 650
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYilGLTALHSSIKS 279
                         330       340
                  ....*....|....*....|
gi 62862424   651 gyEDVAKILVRHGIDTDCWD 670
Cdd:PHA02878  280 --ERKLKLLLEYGADINSLN 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
717-865 1.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   717 DEAQDKaSPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLcHPDIDLKLRDKSGNTPFATA 796
Cdd:PHA02878  164 DRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   797 LDF-RNHNAAQRILDRFPTAAEQMDIRGRNFLHLAILKDDLESVlfLLAIQVDVNSRvhDANQSSPLHLA 865
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLKL--LLEYGADINSL--NSYKLTPLSSA 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
721-781 1.78e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62862424   721 DKASPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDID 781
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
508-777 1.96e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   508 LHIAVEANAIDALEAFVELknkshDIDFNCQDINGDSPLSLCLSLKRTTLVPTLIRggsdvnGKNKNNLSPLHQSIK--- 584
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTR-----GHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR------SINKCSVFYTLVAIKdaf 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   585 ------------------NEDSD----------------ISLFLLEQGADITALTENLD-SALDLSIKHDLSEVVDALCR 629
Cdd:PHA02878  110 nnrnveifkiiltnryknIQTIDlvyidkkskddiieaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   630 RGIALSI-NKNGESPLWSALEKGYEDVAKILVRHGIDTDCWDEgpegCRQTLLHRAIDE--NKESVAIFLIQSQCDLDSS 706
Cdd:PHA02878  190 YGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK----CGNTPLHISVGYckDYDILKLLLEHGVDVNAKS 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424   707 RQPGpngeggdeaqdkASPLHLCCHwgQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYD-EIISILLCH 777
Cdd:PHA02878  266 YILG------------LTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCiNIGRILISN 323
BTB_POZ_BPM_plant cd18280
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
85-163 2.12e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in plant BTB/POZ-MATH (BPM) protein family; The BPM protein family includes Arabidopsis thaliana BTB/POZ and MATH domain-containing proteins, AtBPM1-6, and similar proteins from other plants. BPM protein, also called protein BTB-POZ and MATH domain, may act as a substrate-specific adaptor of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349589 [Multi-domain]  Cd Length: 121  Bit Score: 47.71  E-value: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   85 FPAHKIVLHARSEKWGNDLLS-----NIQQLDWSDLNEDVVLSLLRWIYTD-LIDLQ----NDGLALD------LLKAAH 148
Cdd:cd18280   26 FRAHKLVLAARSPVFRSMLFGpmreeNEGEIVIEDVEPPVFKALLHFIYKDeLPDDVepagSDSSSLDttmaqhLLAAAD 105
                         90
                 ....*....|....*
gi 62862424  149 RFGLPSLLGICERAL 163
Cdd:cd18280  106 RYALERLRLLCESRL 120
FYVE_ZFY19 cd15749
FYVE-related domain found in FYVE domain-containing protein 19 (ZFY19) and similar proteins; ...
1063-1113 2.15e-06

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: 45.57  E-value: 2.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGiNKPVRVCTVCF 1113
Cdd:cd15749    2 CFGCAAKFSLFKKECGCKNCGRSFCKGCLTFSAVVPRKG-NQKQKVCKQCH 51
BTB_POZ_TDPOZ cd18344
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-171 3.78e-06

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in TD and POZ domain-containing proteins (TDPOZ); TDPOZ is a family of bipartite animal and plant proteins that contains a tumor necrosis factor receptor-associated factor (TRAF) domain (TD) and a POZ/BTB domain. TDPOZ proteins may be nuclear scaffold proteins probably involved in transcription regulation in early development and other cellular processes. This subfamily contains only mammalian members. Plant TDPOZ proteins contain a MATH domain at the N-terminal region and are named "BTB/POZ and MATH domain-containing proteins (BPM)", not included in this subfamily. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349653 [Multi-domain]  Cd Length: 128  Bit Score: 47.26  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYADIYIRSQTRVFPAHKIVLHARS-------EKWGNDLLSNIQQLdwSDLNEDVVLSLLRWIYTDLI-DLQ 135
Cdd:cd18344   14 LGELWENSLFTDCCLLVAGHEFRAHKAILAARSpvframfEHEMEERLKNPIEI--HDLDPQVFKEMMGFIYTGKApHLH 91
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 62862424  136 NDGLALDLLKAAHRFGLPSLLGICERALVTSVGVRS 171
Cdd:cd18344   92 SHSMACDVLAAADKYGLEGLKVLCEDALCRNLSVEN 127
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
351-494 4.18e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   351 ILQRQLNINIQNIKGETPLHIAIARRNVEMVKLLLKvPNIDINLRTYDEKCALELSLSMGDHEflIASILLSMGARTDrt 430
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISAKHHK--IFRILYHFASISD-- 618
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424   431 nSKTGDSLLQVFAldrHRGEKSAI--FLADFADLDHINFRGLTALHIAALNNMPNLVKKLIVNGAS 494
Cdd:PLN03192  619 -PHAAGDLLCTAA---KRNDLTAMkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_2 pfam12796
Ankyrin repeats (3 copies);
262-395 5.26e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    262 LEMALSSKNAKIAKSLVDNGmANINAVNMEGfsllksalkngdafsanflldqnclldlpskpssDTALHIICNYGpdnt 341
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNG----------------------------------RTALHLAAKNG---- 41
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62862424    342 peIMEVVkKILQRQLNINIQNiKGETPLHIAIARRNVEMVKLLLKvPNIDINLR 395
Cdd:pfam12796   42 --HLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLE-KGADINVK 90
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
275-385 5.87e-06

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: 50.46  E-value: 5.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    275 KSLVDNGMANINAVNMEGFSLLKSALKNGDAFS-ANFLLDQNCLLDLpskpsSDTALHIICNYGPDNTPEIMEVVKKILQ 353
Cdd:TIGR00870   35 RDLEEPKKLNINCPDRLGRSALFVAAIENENLElTELLLNLSCRGAV-----GDTLLHAISLEYVDAVEAILLHLLAAFR 109
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 62862424    354 RQLNINIQN-------IKGETPLHIAIARRNVEMVKLLL 385
Cdd:TIGR00870  110 KSGPLELANdqytsefTPGITALHLAAHRQNYEIVKLLL 148
FYVE_protrudin cd15723
FYVE-related domain found in protrudin and similar proteins; Protrudin, also termed zinc ...
1063-1112 6.48e-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: 44.80  E-value: 6.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424 1063 CQHCTNRFT-ITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKP------VRVCTVC 1112
Cdd:cd15723    2 CTGCGASFSvLLKKRRSCNNCGNAFCSRCCSKKVPRSVMGATAPaaqretVFVCSGC 58
PHA02875 PHA02875
ankyrin repeat protein; Provisional
484-702 7.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 7.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   484 LVKKLIVNGASSNLKHIDcgLKSALHIAVEANAIDALEAFVELKNKSHDIDFNcqdiNGDSPLSLCLSLKRTTLVPTLIR 563
Cdd:PHA02875   50 AIKLLMKHGAIPDVKYPD--IESELHDAVEEGDVKAVEELLDLGKFADDVFYK----DGMTPLHLATILKKLDIMKLLIA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   564 GGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGAditalTENLDSALdlsikhdlsevvdalcrrgialsinknGESP 643
Cdd:PHA02875  124 RGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA-----CLDIEDCC---------------------------GCTP 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424   644 LWSALEKGYEDVAKILVRHGIDTDCWDEGPEgcrQTLLHRAIDENKESVAIFLIQSQCD 702
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGC---VAALCYAIENNKIDIVRLFIKRGAD 227
FYVE_MTMR_unchar cd15738
FYVE-related domain found in uncharacterized myotubularin-related proteins mainly from ...
1066-1113 9.83e-06

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: 44.24  E-value: 9.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 62862424 1066 CTNRFTITMRKHHCRHCGRVLCSKCSCNDVPILKFGINKPVRVCTVCF 1113
Cdd:cd15738   14 CSTPFDHFSKKHHCWRCGNVFCTRCIDKQRALPGHLSQRPVPVCRACY 61
BTB_POZ_BTBD3_6 cd18282
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
82-166 1.33e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD3 and BTBD6; This family includes BTB/POZ domain-containing proteins BTBD3 and BTBD6, both of which are BTB-domain-containing Kelch-like proteins. BTBD3 controls dendrite orientation toward active axons in mammalian neocortex. BTBD6 is required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349591 [Multi-domain]  Cd Length: 108  Bit Score: 45.08  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   82 TRVFPAHKIVLHARSE----KWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGLaLDLLKAAHRFGLPSLLG 157
Cdd:cd18282   20 TQRIPAHKYVLATGSSvfyaMFYGGLAENKNEIEIPDVEPAAFLNLLRYLYCDEIDLEPDTV-LATLYAAKKYLVPHLAR 98

                 ....*....
gi 62862424  158 ICERALVTS 166
Cdd:cd18282   99 ACVQFLETS 107
BTB1_POZ_ABTB1_BPOZ1 cd18295
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
65-156 1.62e-05

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Ankyrin repeat and BTB/POZ domain-containing protein 1 (ABTB1); ABTB1, also called elongation factor 1A-binding protein or bood POZ containing gene type 1 (BPOZ-1), is an anti-proliferative factor that may act as a mediator of the phosphatase and tensin homolog (PTEN) growth-suppressive signaling pathway. It may play a role in developmental processes. ABTB1 contains an ankyrin repeat and two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349604 [Multi-domain]  Cd Length: 119  Bit Score: 45.32  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   65 ASLFDKNTYADIYIRSQTRVFPAHKIVLHARSE--------KWGNDLLSNIQQldwSDLNEDVVLSLLRWIYTDLIDLQN 136
Cdd:cd18295   11 RRLLEQGSYSDVTFNVHGESFPAHRCILSARSPyfaemfetKWKDKREINLKH---PLVNPDAFRALLQYLYTGRLEIHV 87
                         90       100
                 ....*....|....*....|
gi 62862424  137 DGLAlDLLKAAHRFGLPSLL 156
Cdd:cd18295   88 DDVE-DCKRLAKQCRLEELI 106
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
823-932 1.73e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  823 GRNFLHLAILKDDLESVLFLLA-----IQVDVNSRVHDAnqSSPLHLAAASQNEMITRNLILAGARMNE--------RDA 889
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQG--ETALHIAVVNQNLNLVRELIARGADVVSpratgtffRPG 128
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 62862424  890 VQKL------PLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAV 932
Cdd:cd22192  129 PKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
866-965 1.80e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   866 AASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELLT 945
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
                          90       100
                  ....*....|....*....|....*.
gi 62862424   946 ESR------VNAEATNLKGRNPLHEL 965
Cdd:PTZ00322  170 HSQchfelgANAKPDSFTGKPPSLED 195
BTB_POZ_SPOPL cd18343
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-171 1.92e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein-like (SPOPL); SPOPL, also called HIB homolog 2 or Roadkill homolog 2, is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The complexes may contain homodimeric SPOPL or the heterodimers formed by speckle-type POZ protein (SPOP) and SPOPL, which are less efficient than ubiquitin ligase complexes containing only SPOP. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349652 [Multi-domain]  Cd Length: 123  Bit Score: 45.38  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYAD--IYIRSQTrvFPAHKIVLHARSEKWgNDLL------SNIQQLDWSDLNEDVVLSLLRWIYTDLIDlQ 135
Cdd:cd18343   12 LGNLWENSRFTDcsLFVGGQE--FKAHKSILAARSPVF-NAMFehemeeSKKNRVEINDVDPEVFKEMMRFIYTGKAP-N 87
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 62862424  136 NDGLALDLLKAAHRFGLPSLLGICERALVTSVGVRS 171
Cdd:cd18343   88 LDKMADNLLAAADKYALERLKVMCEEALCNNLSVEN 123
BTB_POZ_KBTBD4 cd18272
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
73-174 2.46e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch repeat and BTB domain-containing protein 4 (KBTBD4); KBTBD4, also called BTB and kelch domain-containing protein 4 (BKLHD4), is a BTB-BACK-Kelch domain protein belonging to a large family of cullin-RING ubiquitin ligase adaptors that facilitate the ubiquitination of target substrates. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349581 [Multi-domain]  Cd Length: 140  Bit Score: 45.27  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   73 YADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQ-----LDWSDLNEDVVLSLLRWIYTDLIDLQNDGLAlDLLKAA 147
Cdd:cd18272   32 FADVTISVEGKEFQLHRLVLSAQSCFFRSMFTSNLKEarnrvIELKDVSESVFQLLVDYIYHGTVKLRVEELQ-ETYEVA 110
                         90       100
                 ....*....|....*....|....*..
gi 62862424  148 HRFGLPSLLGICERALVTSVGVRSCIR 174
Cdd:cd18272  111 DMYQLTALFEECSRFLARTVQVRNCLQ 137
BTB_POZ_ARIA_plant cd18352
BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in ...
72-171 2.78e-05

BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ (poxvirus and zinc finger) domain found in plant ARM repeat protein interacting with ABF2 (ARIA) and similar proteins; ARIA is an armadillo (ARM) repeat and BTB domain-containing protein that acts as a positive regulator of ABA response via the modulation of the transcriptional activity of ABF2, a transcription factor which controls ABA-dependent gene expression via the G-box-type ABA-responsive elements. ARIA is a novel abscisic acid signaling component. It negatively regulates seed germination and young seedling growth. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349661 [Multi-domain]  Cd Length: 116  Bit Score: 44.39  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   72 TYADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDgLALDLLKA 146
Cdd:cd18352   12 TLSDVTFLVEGRRFYAHRIALLASSDAFramfdGGYREKEARDIEIPNIRWEVFELMMRFIYTGSVDITND-IAKDLLRA 90
                         90       100
                 ....*....|....*....|....*
gi 62862424  147 AHRFGLPSLLGICERALVTSVGVRS 171
Cdd:cd18352   91 ADQYLLEGLKRLCEYTIAQDLTLEN 115
PHA03100 PHA03100
ankyrin repeat protein; Provisional
736-944 3.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   736 KVLQTLIDHGANVNLIDAESKSPLHVAIESQYD-----EIISILLCHpDIDLKLRDKSGNTPFATALD--FRNHNAAQRI 808
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY-GANVNAPDNNGITPLLYAISkkSNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   809 LDRfptaAEQMDI---RGRNFLHLAI--LKDDLESVLFLLAIQVDVNSrvhdanqssplhlaaasqnemITR-NLILA-G 881
Cdd:PHA03100  128 LDN----GANVNIknsDGENLLHLYLesNKIDLKILKLLIDKGVDINA---------------------KNRvNYLLSyG 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62862424   882 ARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRELL 944
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
BTB1_POZ_RhoBTB cd18299
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
67-163 4.16e-05

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing proteins (RhoBTB); RhoBTB proteins constitute a subfamily of atypical members within the Rho family of small guanosine triphosphatases (GTPases), which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. In vertebrates, the RhoBTB subfamily consists of 3 isoforms: RhoBTB1, RhoBTB2, and RhoBTB3. Orthologs are present in several other eukaryotes, such as Drosophila and Dictyostelium, but have been lost in plants and fungi. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349608 [Multi-domain]  Cd Length: 103  Bit Score: 43.74  E-value: 4.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRV-FPAHKIVLHARSEKWgNDLLSN--IQQLDwSDLNEDVVLSLLRWIYTDLIDLQNDGLAlDL 143
Cdd:cd18299    6 LLHSPSCADVVFILQGGVrIFAHRIVLAAASSVF-ADLFLMmtVVTLD-SDITPEAFRRVLEFLYTGVLDENEDDLK-EL 82
                         90       100
                 ....*....|....*....|
gi 62862424  144 LKAAHRFGLPSLLGICERAL 163
Cdd:cd18299   83 KDAAELLELFDLVMMCTNVL 102
BTB_POZ_RCBTB1_2 cd18298
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
63-163 4.23e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2; The RCC1-related guanine nucleotide exchange factor (GEF) family includes RCC1 and BTB domain-containing proteins, RCBTB1 and RCBTB2, both of which are chromosome condensation regulator-like guanine nucleotide exchange factors. They contain an RCC1 repeat, a BTB domain, and a BACK domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349607 [Multi-domain]  Cd Length: 108  Bit Score: 43.78  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   63 TVASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKwgndlLSNIQQLDWSDLNEDVVL----------SLLRWIYTDLI 132
Cdd:cd18298    2 SLRKAFNDPRTSDLKFRVDGKYIYVHKAILKIRCEY-----FRSMFQSHWNEDDKNVIEidqysypvyyAFLRYLYTDQV 76
                         90       100       110
                 ....*....|....*....|....*....|..
gi 62862424  133 DL-QNDglALDLLKAAHRFGLPSLLGICERAL 163
Cdd:cd18298   77 DLpPED--AIGLLDLANSYCEERLKKLCEDII 106
Ank_5 pfam13857
Ankyrin repeats (many copies);
354-405 4.62e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62862424    354 RQLNINIQNIKGETPLHIAIARRNVEMVKLLLKvPNIDINLRTYDEKCALEL 405
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDL 55
PHA02875 PHA02875
ankyrin repeat protein; Provisional
582-775 4.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   582 SIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGIALSINKNG-ESPLWSALEKGYEDVAKILV 660
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   661 RHG--IDTDCWDEGpegcrQTLLHRAIDENKESVAIFLIQSQCDLDSSrqpgpngeggdeAQDKASPLHLCCHWGQTKVL 738
Cdd:PHA02875   89 DLGkfADDVFYKDG-----MTPLHLATILKKLDIMKLLIARGADPDIP------------NTDKFSPLHLAVMMGDIKGI 151
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 62862424   739 QTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILL 775
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
BTB_POZ_BTBD6 cd18349
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
66-167 5.01e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 6 (BTBD6); BTBD6, also termed lens BTB domain protein, is a BTB-domain-containing Kelch-like protein required for proper embryogenesis and plays an essential evolutionary conserved role during neuronal development. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349658 [Multi-domain]  Cd Length: 109  Bit Score: 43.43  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   66 SLFDKNTYADIYI----RSQTRVFPAHKIVLHARSEKWG----NDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQND 137
Cdd:cd18349    1 LMFNNELMADVHFivgpPGASQRVPAHKYVLAVGSSVFYamfyGDLAEVKSEIHIPDVEPAAFLILLKYMYSDEIDLEAD 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 62862424  138 GLaLDLLKAAHRFGLPSLLGICERALVTSV 167
Cdd:cd18349   81 TV-LATLYAAKKYIVPALAKACVNFLETSL 109
PHA02874 PHA02874
ankyrin repeat protein; Provisional
222-395 5.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   222 KTKHPLHAAVRLLREDVVSLCIqKYGNSlVNTFSENGILPLEMALSSKNAKIAKSLVDNGmANINAVNMEGFSLLKSALK 301
Cdd:PHA02874  123 ELKTFLHYAIKKGDLESIKMLF-EYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAE 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   302 NGDAFSANFLLDQNCLLDLPSKpSSDTALHIICNYGPDNTPeimevvkkILQRQLNINIQNIKGETPLHIAIARR-NVEM 380
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHNRSAIE--------LLINNASINDQDIDGSTPLHHAINPPcDIDI 270
                         170
                  ....*....|....*
gi 62862424   381 VKLLLkVPNIDINLR 395
Cdd:PHA02874  271 IDILL-YHKADISIK 284
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
755-897 5.98e-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: 47.31  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  755 SKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRNHNAAQRILDRFPTAA-EQMD---IRGRNFLHLA 830
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnEPMTsdlYQGETALHIA 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424  831 ILKDDLESVLFLLAIQVDVNS--------RVHDANQ----SSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHI 897
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSpratgtffRPGPKNLiyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
BTB_POZ_BTBD12_SLX4 cd18288
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
84-160 6.03e-05

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Structure-specific endonuclease subunit SLX4; SLX4, also called BTB/POZ domain-containing protein 12 (BTBD12), is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleases and is required for DNA repair. Mutations of the SLX4 gene are found in Fanconi anemia. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349597 [Multi-domain]  Cd Length: 116  Bit Score: 43.61  E-value: 6.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   84 VFPAHKIVLHAR---------SEKWG--NDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNdGLALDLLKAAHRFGL 152
Cdd:cd18288   30 VLYAHSFVLYARcplliqmvhSEGFSveEEGGVTTRRVLLGDVSGEAARCFLQYLYTADTGLPP-GLSPHVSELADRFGV 108

                 ....*...
gi 62862424  153 PSLLGICE 160
Cdd:cd18288  109 SELVHLCE 116
Ank_4 pfam13637
Ankyrin repeats (many copies);
724-775 6.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62862424    724 SPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILL 775
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
309-611 9.72e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   309 NFLLDQNCLLDLPSKpSSDTALHI-ICNygpDNTPEIMEVvkkILQRQLNINIQNIKGETPLHIAIARRNV--EMVKLLL 385
Cdd:PHA03095   67 RLLLEAGADVNAPER-CGFTPLHLyLYN---ATTLDVIKL---LIKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   386 KVpNIDINLRTYDEKCALELSLSMGDHEFLIASILLSMGARtDRTNSKTGDSLLQVFALDRH-RGEKSAIFLADFADLDH 464
Cdd:PHA03095  140 RK-GADVNALDLYGMTPLAVLLKSRNANVELLRLLIDAGAD-VYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPAA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   465 INFRGLTALHIAAlnnMPNLVKKLIVngasSNLkhidcglksalhiaVEANaidaleafvelknkshdIDFNCQDINGDS 544
Cdd:PHA03095  218 TDMLGNTPLHSMA---TGSSCKRSLV----LPL--------------LIAG-----------------ISINARNRYGQT 259
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424   545 PLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSA 611
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTA 326
BTB2_POZ_BTBD8 cd18286
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
67-177 1.05e-04

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 8 (BTBD8); BTBD8 is a BTB-domain-containing Kelch-like protein that may play a role in developmental processes. It may also act as a protein-protein adaptor in a transcription complex and thus be involved in brain development. BTBD8 contains two BTB domains. This model corresponds to the second domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349595 [Multi-domain]  Cd Length: 121  Bit Score: 43.02  E-value: 1.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   67 LFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWgNDLLSNiqqlDWSDLNEDV----------VLSLLRWIYTDLIDLQN 136
Cdd:cd18286   11 LFLNGEDSDITIKVDGKTFKAHRCILCARSSYF-AAMLSG----SWAESNSSEitltgvshaaVSFVLLFIYGGVLDLPD 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 62862424  137 DGLALDLLKAAHRFGLPSLLGICERALvtsvgvrscIRFYC 177
Cdd:cd18286   86 DVNLGELLSLADMYGLDGLKDVVAYTL---------RRDYC 117
Ank_4 pfam13637
Ankyrin repeats (many copies);
858-911 1.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 62862424    858 QSSPLHLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALI 911
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
224-431 1.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   224 KHPLHAAVrlLREDVVS----LCIQKYGNslvNTFSENGILPLEMALSSKNAKIAKSLVDNGmANINAVNMEGFSLLKSA 299
Cdd:PHA02875   69 ESELHDAV--EEGDVKAveelLDLGKFAD---DVFYKDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   300 LKNGDAFSANFLLDQNCLLDLPSKPSSdTALHIICNYGPdntpeiMEVVKKILQRQLNINIQNIKGE-TPLHIAIARRNV 378
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGC-TPLIIAMAKGD------IAICKMLLDSGANIDYFGKNGCvAALCYAIENNKI 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424   379 EMVKLLLKvPNIDINL---------RTYDEKCALELSLSMGDHEFLIASILLSMGARTDRTN 431
Cdd:PHA02875  216 DIVRLFIK-RGADCNImfmiegeecTILDMICNMCTNLESEAIDALIADIAIRIHKKTIRRD 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
366-494 1.67e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  366 ETPLHIAIARRNVEMVKLLLKVPNIDINLRtydekcalelslsmgdhefliasillsmGArtdrtnskTGDSLLQVFALD 445
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQR----------------------------GA--------LGETALHVAALY 61
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 62862424  446 RHRgeKSAIFLADfADLDHIN-------FRGLTALHIAALNNMPNLVKKLIVNGAS 494
Cdd:cd22192   62 DNL--EAAVVLME-AAPELVNepmtsdlYQGETALHIAVVNQNLNLVRELIARGAD 114
PHA02874 PHA02874
ankyrin repeat protein; Provisional
219-385 1.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   219 LKTKTKHPLHAAVRLLREDVVSLCIqkygnslvntfsENGILPLEMALSSKNAKIAKSLVDNGMaNINAVNMEGFSLLKS 298
Cdd:PHA02874   64 INTKIPHPLLTAIKIGAHDIIKLLI------------DNGVDTSILPIPCIEKDMIKTILDCGI-DVNIKDAELKTFLHY 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   299 ALKNGDAFSANFLLDQNCLLDLPSKpSSDTALHIICNYgpdntpEIMEVVKKILQRQLNINIQNIKGETPLHIAIARRNV 378
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDD-NGCYPIHIAIKH------NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203

                  ....*..
gi 62862424   379 EMVKLLL 385
Cdd:PHA02874  204 ACIKLLI 210
Ank_5 pfam13857
Ankyrin repeats (many copies);
893-931 1.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.92e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 62862424    893 LPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIA 931
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
541-775 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   541 NGDSPLSLCLSLKRTTLVPTLIRGGSDVNGKNKNNLSPLHQSIknedsdislfllEQGaDITALTENLDSAldlSIKHDL 620
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAV------------EEG-DVKAVEELLDLG---KFADDV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   621 sevvdalcrrgialsINKNGESPLWSALEKGYEDVAKILVRHGIDTDCwdegPEGCRQTLLHRAIDENKESVAIFLIQSQ 700
Cdd:PHA02875   98 ---------------FYKDGMTPLHLATILKKLDIMKLLIARGADPDI----PNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62862424   701 CDLDSSRQPGpngeggdeaqdkASPLHLCCHWGQTKVLQTLIDHGANVNLIdaeSKSP----LHVAIESQYDEIISILL 775
Cdd:PHA02875  159 ACLDIEDCCG------------CTPLIIAMAKGDIAICKMLLDSGANIDYF---GKNGcvaaLCYAIENNKIDIVRLFI 222
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
794-1029 2.12e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   794 ATALDFRNHNAAQriLDRFPTAA--EQMDIRG-------RNFL-HLAILKD-DLESVLFllaiqvDVNSRVHDANQSSPL 862
Cdd:PLN03192  458 PQSFTFRTKTLSQ--LLRLKTSTliEAMQTRQednvvilKNFLqHHKELHDlNVGDLLG------DNGGEHDDPNMASNL 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   863 HLAAASQNEMITRNLILAGARMNERDAVQKLPLHIAIERGNLPAVSALIQNNADYDATDADGNNALHIAVRCAQFFIVRE 942
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   943 LLTESRvnaeATNLKGRNPLheLCRVVEDSTAGLICELFlesmpKYPINI--PDMDGNTPLLLSFMRGQSPLCKILVKAG 1020
Cdd:PLN03192  610 LYHFAS----ISDPHAAGDL--LCTAAKRNDLTAMKELL-----KQGLNVdsEDHQGATALQVAMAEDHVDMVRLLIMNG 678

                  ....*....
gi 62862424  1021 ACLGTENKD 1029
Cdd:PLN03192  679 ADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
639-810 2.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   639 NGESPLWSALEKGYEDVAKILVRHGIDTDCWDEGPEgcrqTLLHRAIDENKESVAIFLIQSQCDLDSSRQpgpngeggde 718
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE----SELHDAVEEGDVKAVEELLDLGKFADDVFY---------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   719 aQDKASPLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVAIESQYDEIISILLCHPDIdLKLRDKSGNTPFATALD 798
Cdd:PHA02875  100 -KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMA 177
                         170
                  ....*....|..
gi 62862424   799 FRNHNAAQRILD 810
Cdd:PHA02875  178 KGDIAICKMLLD 189
PHA02736 PHA02736
Viral ankyrin protein; Provisional
289-428 2.71e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   289 NMEGFSLLKSALKNGDAFS----ANFLLDQNCLLDLPSKPSSDTALHIICNygPDNTPEImEVVKKILQRQLNINIQN-I 363
Cdd:PHA02736   14 DIEGENILHYLCRNGGVTDllafKNAISDENRYLVLEYNRHGKQCVHIVSN--PDKADPQ-EKLKLLMEWGADINGKErV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62862424   364 KGETPLHIAIARRNVEMVKLLLKVPNIDINLRTYDEKCALELSLSMGDHEflIASILLSMGARTD 428
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQPGVNMEILNYAFKTPYYVACERHDAK--MMNILRAKGAQCK 153
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
561-632 3.81e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 3.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424   561 LIRGGSDVNGKNKNNLSPLHQSIKNEDSDISLFLLEQGADITALTENLDSALDLSIKHDLSEVVDALCRRGI 632
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
327-477 3.85e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 3.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  327 DTALHIICNYgpDNtpeiMEVVKKILQ--RQLnINI----QNIKGETPLHIAIARRNVEMVKLLLK-------------- 386
Cdd:cd22192   52 ETALHVAALY--DN----LEAAVVLMEaaPEL-VNEpmtsDLYQGETALHIAVVNQNLNLVRELIArgadvvspratgtf 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  387 -VPNIDiNLRTYDEKcALELSLSMGDHEflIASILLSMGARTdRTNSKTGDSLLQVFALDRHRgeKSA-----IFLA--- 457
Cdd:cd22192  125 fRPGPK-NLIYYGEH-PLSFAACVGNEE--IVRLLIEHGADI-RAQDSLGNTVLHILVLQPNK--TFAcqmydLILSydk 197
                        170       180
                 ....*....|....*....|...
gi 62862424  458 --DFADLDHI-NFRGLTALHIAA 477
Cdd:cd22192  198 edDLQPLDLVpNNQGLTPFKLAA 220
PHA02741 PHA02741
hypothetical protein; Provisional
732-801 4.67e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 4.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62862424   732 WGQTKVLQTLIDHGANVNLIDA-ESKSPLHVAIESQYDEIISILLCHPDIDLKLRDKSGNTPFATALDFRN 801
Cdd:PHA02741   74 QLAAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNED 144
BTB2_POZ_RHOBTB3 cd18360
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
66-165 4.79e-04

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Rho-related BTB domain-containing protein 3 (RhoBTB3); RhoBTB3 is an atypical Rho family small guanosine triphosphatase (GTPase) and is a member of the RhoBTB subfamily, which is characterized by containing a GTPase domain (in most cases, non-functional) followed by a proline-rich region, tandem BTB domains, and a conserved C-terminal region. The carboxyl terminal extension that harbors two BTB domains is capable of assembling cullin 3-dependent ubiquitin ligase complexes. RhoBTB3 is a Golgi-associated Rho-related ATPase that regulates the S/G2 transition of the cell cycle by targeting cyclin E for ubiquitylation. It is involved in vesicle trafficking and in targeting proteins for degradation in the proteasome. It binds directly to Rab9 GTPase and functions with Rab9 in protein transport from endosomes to the trans Golgi network. It also promotes proteasomal degradation of Hypoxia-inducible factor alpha (HIFalpha) through facilitating hydroxylation and suppresses the Warburg effect. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349669 [Multi-domain]  Cd Length: 110  Bit Score: 40.99  E-value: 4.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   66 SLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGLA 140
Cdd:cd18360    3 LFFNSPLLADVVFKIQGTTVPAHRAVLVARCEVMaamfnGNYAEAKSFLVPIYGVSKDTFLSFLEYLYTDSCCPASILQA 82
                         90       100
                 ....*....|....*....|....*
gi 62862424  141 LDLLKAAHRFGLPSLLGICERALVT 165
Cdd:cd18360   83 MALLICAEMYQVSRLQHICELYIIT 107
PHA02946 PHA02946
ankyin-like protein; Provisional
713-900 5.03e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.89  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   713 GEGGDEAQDKAS-PLHLCCHWGQTKVLQTLIDHGANVNLIDAESKSPLHVaIESQYDEIISILLCHPDIDLKLR---DKS 788
Cdd:PHA02946   62 GYSPNETDDDGNyPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIERINLLVQYGAKINnsvDEE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   789 GNTPFATALDfrnhnAAQRILDRFPT---AAEQMDIRGRNFLHLAILKDDLESVLFLLAIQVDVNSRVHDANQSSPLHLA 865
Cdd:PHA02946  141 GCGPLLACTD-----PSERVFKKIMSigfEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 62862424   866 AASQNEMI-TRNLILAGARMNERDAVQKLPLHIAIE 900
Cdd:PHA02946  216 CSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIK 251
PHA02741 PHA02741
hypothetical protein; Provisional
346-406 5.96e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.95  E-value: 5.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62862424   346 EVVKKILQRQLNINIQN-IKGETPLHIAIARRNVEMVKLLLKVPNIDINLRTYDEKCALELS 406
Cdd:PHA02741   78 EIIDHLIELGADINAQEmLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELA 139
BTB_POZ_BTBD1_2 cd18281
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-163 1.11e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing proteins, BTBD1 and BTBD2; This family includes BTB/POZ domain-containing proteins BTBD1 and BTBD2, both of which are BTB-domain-containing Kelch-like proteins that interact with DNA topoisomerase 1 (Topo1), a key enzyme of cell survival. BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349590 [Multi-domain]  Cd Length: 127  Bit Score: 40.11  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYADIYI-----RSQTRVfPAHKIVLHARS----EKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDL 134
Cdd:cd18281   13 FAFLFNNETLSDVHFivgkgDNEQRI-PAHKFVLSIGSavfdAMFNGGMATTSAEIELPDVEPAAFLALLRFLYSDEVQI 91
                         90       100
                 ....*....|....*....|....*....
gi 62862424  135 QNDGLaLDLLKAAHRFGLPSLLGICERAL 163
Cdd:cd18281   92 GPETV-MTTLYTAKKYAVPALESACVEFL 119
PHA02859 PHA02859
ankyrin repeat protein; Provisional
512-607 1.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   512 VEANAIDALEAFVELKNkshdidfNCQDINgDSPLSLCLSLKRTTL--VPTLIRGGSDVNGKNK-NNLSPLHQSI---KN 585
Cdd:PHA02859   29 VEKDDIEGVKKWIKFVN-------DCNDLY-ETPIFSCLEKDKVNVeiLKFLIENGADVNFKTRdNNLSALHHYLsfnKN 100
                          90       100
                  ....*....|....*....|..
gi 62862424   586 EDSDISLFLLEQGADITALTEN 607
Cdd:PHA02859  101 VEPEILKILIDSGSSITEEDED 122
Ank_5 pfam13857
Ankyrin repeats (many copies);
741-796 1.58e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 62862424    741 LIDHG-ANVNLIDAESKSPLHVAIESQYDEIISILLCHPdIDLKLRDKSGNTPFATA 796
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
BTB_POZ_ZBTB32_FAZF_TZFP cd18218
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
65-163 1.64e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in zinc finger and BTB domain-containing protein 32 (ZBTB32); ZBTB32 is also called FANCC-interacting protein, fanconi anemia zinc finger protein (FAZF), testis zinc finger protein (TZFP), or zinc finger protein 538 (ZNF538). It is a DNA-binding transcription factor that binds to the 5'-TGTACAGTGT-3' core sequence. It acts as a transcription suppressor that controls T cell-mediated autoimmunity. ZBTB32 is essential for down-regulation of GATA3 via ZPO2; this promotes aggressive breast cancer development. It contains a BTB/POZ domain, a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349527 [Multi-domain]  Cd Length: 110  Bit Score: 39.15  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   65 ASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLS-NIQQLDWSD-LNEDVVLSLLRWIYTDLIDLQNDGLAlD 142
Cdd:cd18218   10 ARLRPAGALCDTLITVGSQEFPAHSLVLAGASQQLGRQLTNpNPGQWCLGEgISPSTFKQLLDFVYGESVEVQPGELR-P 88
                         90       100
                 ....*....|....*....|.
gi 62862424  143 LLKAAHRFGLPSLLGICERAL 163
Cdd:cd18218   89 LLEAARALEVESLEEACWRAL 109
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
372-498 1.76e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 1.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    372 AIARRNVEMVKLLLKVP-NIDINLRTYDEKCALELSLSMGDHEFLIaSILLSMGARTDrtnskTGDSLLQVFALDRHRGE 450
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPkKLNINCPDRLGRSALFVAAIENENLELT-ELLLNLSCRGA-----VGDTLLHAISLEYVDAV 97
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    451 KSAIFLADFADLDHIN------------FRGLTALHIAALNNMPNLVKKLIVNGASSNLK 498
Cdd:TIGR00870   98 EAILLHLLAAFRKSGPlelandqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02878 PHA02878
ankyrin repeat protein; Provisional
271-397 2.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   271 AKIAKSLVDNGmANINAVNME-GFSLLKSALKNGDAFSANFLLDQNCLLDLPSKPSSDTALHIICNYGPDntpeimeVVK 349
Cdd:PHA02878  147 AEITKLLLSYG-ADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP-------IVH 218
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 62862424   350 KILQRQLNINIQNIKGETPLHIAIAR-RNVEMVKLLLKvPNIDINLRTY 397
Cdd:PHA02878  219 ILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLE-HGVDVNAKSY 266
BTB2_POZ_IBtk cd18302
second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
75-164 3.15e-03

second BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the second BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349611 [Multi-domain]  Cd Length: 113  Bit Score: 38.50  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   75 DIYIRSQT-RVFPAHKIVLHARSEKWGNDLLSNIqqLDWSDLNE-------DVVLSLLRWIYTD----LIDLQNDGLALD 142
Cdd:cd18302    7 DVTIVSEDgKEFPCHKCVLVARLEYFHSMLSSSW--IEASSCSAltmpipsDILEIILDYLYTDeasaVKESQNVEFLCN 84
                         90       100
                 ....*....|....*....|..
gi 62862424  143 LLKAAHRFGLPSLLGICERALV 164
Cdd:cd18302   85 VLVIADQLLITRLKEICEVALV 106
PHA03098 PHA03098
kelch-like protein; Provisional
87-176 3.25e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 41.29  E-value: 3.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424    87 AHKIVLHARSEKWGNDLLSNIQQLDWS-DLNEDVVLSLLRWIYTDLIDLQNDGLAlDLLKAAHRFGLPSLLGICERALVT 165
Cdd:PHA03098   25 VHKIILSSSSEYFKKMFKNNFKENEINlNIDYDSFNEVIKYIYTGKINITSNNVK-DILSIANYLIIDFLINLCINYIIK 103
                          90
                  ....*....|.
gi 62862424   166 SVGVRSCIRFY 176
Cdd:PHA03098  104 IIDDNNCIDIY 114
Ank_5 pfam13857
Ankyrin repeats (many copies);
460-511 3.51e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 62862424    460 ADLDHINFRGLTALHIAALNNMPNLVKKLIVNGASSNLKHIDCglKSALHIA 511
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG--LTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
724-752 3.99e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.99e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 62862424    724 SPLHLCC-HWGQTKVLQTLIDHGANVNLID 752
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
721-750 4.12e-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: 4.12e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 62862424     721 DKASPLHLCCHWGQTKVLQTLIDHGANVNL 750
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
339-385 4.18e-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: 41.28  E-value: 4.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424  339 DNTPEIMEVV------KKILQRQLNINI--QNIKGETPLHIAIARRNVEMVKLLL 385
Cdd:cd22194  107 ENTKEIVRILlafaeeNGILDRFINAEYteEAYEGQTALNIAIERRQGDIVKLLI 161
BTB_POZ_BTBD3 cd18348
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
65-173 4.30e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 3 (BTBD3); BTBD3 is a BTB-domain-containing Kelch-like protein that controls dendrite orientation toward active axons in the mammalian neocortex. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349657 [Multi-domain]  Cd Length: 131  Bit Score: 38.46  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   65 ASLFDKNTYADIYI----RSQTRVFPAHKIVLHARSEKWG----NDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQN 136
Cdd:cd18348   13 AVMFNNDLMADIHFvvgpPGGTQRLPGHKYVLAVGSSVFHamfyGELAEDKDEIRIPDVEPAAFLAMLKYIYCDEIDLAA 92
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 62862424  137 DGLaLDLLKAAHRFGLPSLLGICERALVTSVGVR-SCI 173
Cdd:cd18348   93 DTV-LATLYAAKKYIVPHLARACVNFLETSLSAKnACV 129
BTB_POZ_NS1BP cd18306
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
85-173 5.13e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Influenza virus NS1A-binding protein (NS1-BP); NS1-BP is also called NS1-binding protein, aryl hydrocarbon receptor-associated protein 3 (ARA3), or IVNS1ABP. It is a novel protein that interacts with the influenza A virus nonstructural NS1 protein, which is relocalized in the nuclei of infected cells. It plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through its kelch repeats. It also interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control. NS1-BP contains BTB and BACK domains at the N-terminal region and kelch repeats at the C-terminal region. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349615 [Multi-domain]  Cd Length: 124  Bit Score: 38.01  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   85 FPAHKIVLHARSEKWgNDLLS------NIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDgLALDLLKAAHRFGLPSLLGI 158
Cdd:cd18306   30 IPAHRAVLACASPYL-FELFSsdsdgeSILTVKLDGLDPDAVEVLVNYAYTSRLEVPAD-LVKSVYSAAKKLKMDRVKKA 107
                         90
                 ....*....|....*
gi 62862424  159 CERALVTSVGVRSCI 173
Cdd:cd18306  108 CGDFLLEKLTPQNCI 122
BTB_POZ_SPOP cd18342
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-171 5.25e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in speckle-type POZ protein (SPOP); SPOP, also called HIB homolog 1 or Roadkill homolog 1, is a novel nuclear speckle-type protein which serves as an adaptor of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and proteasomal degradation of target proteins, such as BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349651 [Multi-domain]  Cd Length: 125  Bit Score: 38.16  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYADIYIRSQTRVFPAHKIVLHARSEKWGNDLLSNIQQ-----LDWSDLNEDVVLSLLRWIYTDLIDlQNDG 138
Cdd:cd18342   13 LGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEEskknrVEINDVEPEVFKEMMCFIYTGKAP-NLDK 91
                         90       100       110
                 ....*....|....*....|....*....|...
gi 62862424  139 LALDLLKAAHRFGLPSLLGICERALVTSVGVRS 171
Cdd:cd18342   92 MADDLLAAADKYALERLKVMCEDALCSNLSVEN 124
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
364-396 5.36e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 5.36e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 62862424    364 KGETPLHIAIARR-NVEMVKLLLKVpNIDINLRT 396
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSK-GADVNARD 33
PHA02859 PHA02859
ankyrin repeat protein; Provisional
678-851 5.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   678 QTLLHRAIDENKESVAI--FLIQSQCDLDSsRQPGPNgeggdeaqdkASPLHLCCHWGQT---KVLQTLIDHGANVNLID 752
Cdd:PHA02859   52 ETPIFSCLEKDKVNVEIlkFLIENGADVNF-KTRDNN----------LSALHHYLSFNKNvepEILKILIDSGSSITEED 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   753 AESKSPLHVAIESqydeiisillCHPDID-LKLRDKSGNTPFataldfrnhnaaqrildrfptaaeQMDIRGRNFLHLAI 831
Cdd:PHA02859  121 EDGKNLLHMYMCN----------FNVRINvIKLLIDSGVSFL------------------------NKDFDNNNILYSYI 166
                         170       180
                  ....*....|....*....|.
gi 62862424   832 L-KDDLESVLFLLAIQVDVNS 851
Cdd:PHA02859  167 LfHSDKKIFDFLTSLGIDINE 187
BTB1_POZ_IBtk cd18301
first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain ...
75-145 5.36e-03

first BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in inhibitor of Bruton tyrosine kinase (IBtk); IBtk is an inhibitor or negative regulator of Bruton tyrosine kinase (Btk), which is required for B-cell differentiation and development. IBtk binds to the PH domain of Btk and down-regulates the Btk kinase activity. It contains two BTB domains. This model corresponds to the first BTB domain. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349610 [Multi-domain]  Cd Length: 99  Bit Score: 37.65  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   75 DIYIRSQTRVFPAHKIVLHARS---------EKWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLQNDGLALDLLK 145
Cdd:cd18301   20 DVVFQVGGKTFPAHKFILASRSdyfrklflsSLLTSEDAVGCDVVHIEKVPPEIFEQLLQFIYTDTCDLLTDGYKPKLQR 99
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
895-1009 5.73e-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: 40.90  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  895 LHIAIERGNLPAVSALIQNNADYDA---------TDAD-----GNNALHIAVRCAQFFIVRELLTESRVNAEATNLKGRN 960
Cdd:cd22194  145 LNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNT 224
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62862424  961 PLHELCRVVEDSTA--GLICELF----LESMPKYPINIPDMDGNTPLLLSFMRGQ 1009
Cdd:cd22194  225 VLHALVTVAEDSKTqnDFVKRMYdmilLKSENKNLETIRNNEGLTPLQLAAKMGK 279
BTB_POZ_KLHL1-like cd18234
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
75-173 5.84e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like proteins KLHL1, KLHL4 and KLHL5; This family contains the Kelch-like proteins: KLHL1, KLHL4 and KLHL5, all of which share high identity and similarity with the Drosophila kelch protein, a component of ring canals. KLHL1 is a neuronal actin-binding protein that modulates voltage-gated CaV2.1 (P/Q-type) and CaV3.2 (alpha1H T-type) calcium channels. Family members contain a BTB domain and kelch repeat domains, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349543 [Multi-domain]  Cd Length: 105  Bit Score: 37.73  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   75 DIYIRSQTRVFPAHKIVLHARSE----KWGNDLLSNIQQLDW-SDLNEDVVLSLLRWIYTDLIDLQNDGLAlDLLKAAHR 149
Cdd:cd18234    3 DVILIAGDRRIPAHRLVLSAVSDyfaaMFTNDVREATEEEIKlKDVDPDALWTLVQYCYTGRLELKEDNVE-SLLATACL 81
                         90       100
                 ....*....|....*....|....
gi 62862424  150 FGLPSLLGICERALVTSVGVRSCI 173
Cdd:cd18234   82 LQLSEVVEACCGFLMKQLHPSNCL 105
FYVE_CARP cd15750
FYVE-like domain found in caspase-associated ring proteins, CARP1 and CARP2; CARP1 and CARP2 ...
1063-1091 6.22e-03

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: 35.80  E-value: 6.22e-03
                         10        20
                 ....*....|....*....|....*....
gi 62862424 1063 CQHCTNRFTITMRKHHCRHCGRVLCSKCS 1091
Cdd:cd15750    3 CESCGAKFSVFKRKRTCADCKRYFCSNCL 31
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
364-393 6.30e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.30e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 62862424    364 KGETPLHIAIARRNVEMVKLLLKvPNIDIN 393
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLE-NGADIN 29
BTB_POZ_BTBD17 cd18292
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
64-161 6.87e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in BTB/POZ domain-containing protein 17 (BTBD17); BTBD17, also called galectin-3-binding protein-like, is a BTB domain-containing protein. Its function remains unclear. It may be associated with hepatocellular carcinoma. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349601 [Multi-domain]  Cd Length: 114  Bit Score: 37.65  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   64 VASLFDKNTYADIYIRSQTRVFPAHKIVLHARSE--------KWGNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLq 135
Cdd:cd18292    8 IAQLYNNEELSDIVLRVGGKVFHAHRLILAKSSDvfrvmlsnDWWSESKQSEIELVEDPECAAVFEKFLRYLYTGQISV- 86
                         90       100
                 ....*....|....*....|....*.
gi 62862424  136 NDGLALDLLKAAHRFGLPSLLGICER 161
Cdd:cd18292   87 NLETALPLLMLADKYNVTDLKQLCVD 112
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
822-932 7.43e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 7.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424  822 RGRNFLHLAILKDDLESVLFLLAIQVDVNSRVH-DANQSSPlhlaaasqnemitRNLILAGarmnerdavqKLPLHIAIE 900
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgRFFRKSP-------------GNLFYFG----------ELPLSLAAC 128
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 62862424  901 RGNLPAVSALIQNNAD---YDATDADGNNALHIAV 932
Cdd:cd21882  129 TNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALV 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
364-392 8.20e-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: 34.87  E-value: 8.20e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 62862424     364 KGETPLHIAIARRNVEMVKLLL-KVPNIDI 392
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLdKGADINA 30
BTB_POZ_KLHL7 cd18237
BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in ...
69-173 9.25e-03

BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in Kelch-like protein 7 (KLHL7); KLHL7 is a component of a Cul3-based E3 ubiquitin ligase complex and is involved in the ubiquitination of target proteins for proteasome-mediated degradation. Mutations in KLHL7 causes autosomal-dominant retinitis pigmentosa. It contains a BTB domain and kelch repeats, characteristics of a kelch family protein. The BTB/POZ domain is a common protein-protein interaction motif of about 100 amino acids.


Pssm-ID: 349546 [Multi-domain]  Cd Length: 126  Bit Score: 37.47  E-value: 9.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62862424   69 DKNTYADIYIRSQTRVFPAHKIVLHARSEKW-----GNDLLSNIQQLDWSDLNEDVVLSLLRWIYTDLIDLqNDGLALDL 143
Cdd:cd18237   17 KQKTLCDVILIVEGREIKAHRVVLAAASHFFhlmftSNMTESKSSEVELKDAEPDIIELLVEFAYTARISV-NSNNVQSL 95
                         90       100       110
                 ....*....|....*....|....*....|
gi 62862424  144 LKAAHRFGLPSLLGICERALVTSVGVRSCI 173
Cdd:cd18237   96 LDAANQYQIEPVKKMCVDFLKEQLDASNCL 125
 
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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