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Conserved domains on  [gi|162312211|ref|NP_595759|]
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beige protein 1 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 1919-2202 6.82e-173

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


:

Pssm-ID: 214982  Cd Length: 280  Bit Score: 531.80  E-value: 6.82e-173
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1919 TKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLL 1998
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1999 LglnDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSKENMADVRELIPEFFYL 2078
Cdd:smart01026   81 E---DPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYL 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   2079 SEMFINGNGFDFGSRQkESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFH 2158
Cdd:smart01026  158 PEFLVNINGFDFGTRQ-DGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFH 236

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 162312211   2159 HLSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:smart01026  237 PLTYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 1738-1871 4.75e-19

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 275391  Cd Length: 112  Bit Score: 84.59  E-value: 4.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1738 DSIQDVYNVSRIFGLEATEGILLLGKQYLYLMDNFFLRSDNEIVDVNDNSIIDERDPYLqllhlqslsssgkvrrhiske 1817
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKEHLV--------------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162312211 1818 nnWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLtiLS-NTKNRDSLYQKLVA 1871
Cdd:cd01201    60 --FKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYF--LNfPSKERNDVYKKLLS 110
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2255-2466 2.65e-13

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 73.14  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2255 FAADYTPLGPntFLAWGRVDNTVQLIsDQLDKQPVMFEELHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIkas 2333
Cdd:cd00200    13 TCVAFSPDGK--LLATGSGDGTIKVW-DLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDKTIRLWDLETGECV--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2334 lkRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIqtiavnarnaeiafstgfYCCVVNVN 2413
Cdd:cd00200    87 --RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWV------------------NSVAFSPD 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312211 2414 GKILV---KDKLSRIYNENS----------DENILCSCFYTGANSewlhknlFITGHPDGIIRIWE 2466
Cdd:cd00200   147 GTFVAsssQDGTIKLWDLRTgkcvatltghTGEVNSVAFSPDGEK-------LLSSSSDGTIKLWD 205
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 2556-2600 1.16e-08

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: 53.30  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162312211 2556 CSLCDSRFSLMEWRSQCRACGNSnVCSDCVS-------MLKDTNIKTCYECY 2600
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRV-FCSKCSSkklplpsFGSGKPVRVCDSCY 52
Laminin_G_3 super family cl48183
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 380-534 3.12e-05

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


The actual alignment was detected with superfamily member pfam13385:

Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 46.22  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   380 TLSSPVMPINGYSVSLWLNIESLMNDDGNYAPTTlflisdflKSTLFRLLLDASKKTVVVHIGSSKDTCVVNFSTPITnf 459
Cdd:pfam13385    8 TLPDALLPTSDFTVSAWVKPDSLPGWARAIISSS--------GGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSGASVP-- 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312211   460 fskiykDNpslnppSWHLITLVHRNEksslpNLELYIDGSAVERAACPYPFLSSTLQPLYvslgpsIGSRNQSTP 534
Cdd:pfam13385   78 ------LG------QWTHVAVTYDGG-----TLRLYVNGVLVGSSTLTGGPPPGTGGPLY------IGRSPGGDD 129
DUF4704 super family cl24375
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 715-882 4.41e-04

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


The actual alignment was detected with superfamily member pfam15787:

Pssm-ID: 464870  Cd Length: 486  Bit Score: 45.35  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   715 GSVTPIIMQSISDAIYNIGGSSILLELV-------------GTAETEAELNFGLQVFFSS-IEDNWRFSENVEQTHSFEI 780
Cdd:pfam15787   13 GGVQLCVTHSIHSILYSVGGIQVLFPLFsqldqpvedeqlpGTSEADYSLCATLLSLIADlLESSPTNQQQMHQLRGFLV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   781 LAQILHSKSHLLVSEETLKIIALMsgvhhTRFKHPLVMNPLLFR----YLILDFDLWSKAPnSNLFVQQLGYIVSLIENN 856
Cdd:pfam15787   93 LGYLLQSASPKHLTLEVLNALLSL-----AKVLVSLPTSEVLLKdlfdHILFNPKLWIYTD-YEVQKKLYSYLATDFVSD 166

                          170       180
                   ....*....|....*....|....*.
gi 162312211   857 DYAGFNVKRLMKMQilkKLLTAMRNC 882
Cdd:pfam15787  167 SRIYTNVRRVSTVQ---RLLDTLKQF 189
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 1919-2202 6.82e-173

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


Pssm-ID: 214982  Cd Length: 280  Bit Score: 531.80  E-value: 6.82e-173
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1919 TKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLL 1998
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1999 LglnDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSKENMADVRELIPEFFYL 2078
Cdd:smart01026   81 E---DPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYL 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   2079 SEMFINGNGFDFGSRQkESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFH 2158
Cdd:smart01026  158 PEFLVNINGFDFGTRQ-DGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFH 236

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 162312211   2159 HLSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:smart01026  237 PLTYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
1920-2202 1.68e-169

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 522.04  E-value: 1.68e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  1920 KRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLLl 1999
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEEL- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  2000 glnDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSkENMADVRELIPEFFYLS 2079
Cdd:pfam02138   80 ---EDDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  2080 EMFINGNGFDFGSRQkESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFHH 2159
Cdd:pfam02138  156 EFLLNSNNFDLGGRQ-DGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 162312211  2160 LSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:pfam02138  235 LTYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 1919-2202 4.91e-144

BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.


Pssm-ID: 100117 [Multi-domain]  Cd Length: 275  Bit Score: 449.39  E-value: 4.91e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1919 TKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLl 1998
Cdd:cd06071     1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYES- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1999 lgLNDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSkENMADVRELIPEFFYL 2078
Cdd:cd06071    80 --DSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2079 SEMFINGNGFDFGsrQKESTPINDVILPPWAKGdPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFH 2158
Cdd:cd06071   157 PEFFLNINKFDFG--KQDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFH 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 162312211 2159 HLSYQGAIDLENIENEFElaAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:cd06071   234 PLTYEGSVDLDSIDVERE--AIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 1738-1871 4.75e-19

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275391  Cd Length: 112  Bit Score: 84.59  E-value: 4.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1738 DSIQDVYNVSRIFGLEATEGILLLGKQYLYLMDNFFLRSDNEIVDVNDNSIIDERDPYLqllhlqslsssgkvrrhiske 1817
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKEHLV--------------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162312211 1818 nnWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLtiLS-NTKNRDSLYQKLVA 1871
Cdd:cd01201    60 --FKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYF--LNfPSKERNDVYKKLLS 110
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2255-2466 2.65e-13

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 73.14  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2255 FAADYTPLGPntFLAWGRVDNTVQLIsDQLDKQPVMFEELHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIkas 2333
Cdd:cd00200    13 TCVAFSPDGK--LLATGSGDGTIKVW-DLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDKTIRLWDLETGECV--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2334 lkRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIqtiavnarnaeiafstgfYCCVVNVN 2413
Cdd:cd00200    87 --RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWV------------------NSVAFSPD 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312211 2414 GKILV---KDKLSRIYNENS----------DENILCSCFYTGANSewlhknlFITGHPDGIIRIWE 2466
Cdd:cd00200   147 GTFVAsssQDGTIKLWDLRTgkcvatltghTGEVNSVAFSPDGEK-------LLSSSSDGTIKLWD 205
WD40 COG2319
WD40 repeat [General function prediction only];
2254-2466 2.28e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.40  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2254 AFAADytplgpNTFLAWGRVDNTVQLISDQLDKQPVMFEElHSEKITHV-VACDERTFLTASLDLTLRLWTLSTNKPIka 2332
Cdd:COG2319   127 AFSPD------GKTLASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVaFSPDGKLLASGSDDGTVRLWDLATGKLL-- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2333 slkRVLYGHRYRITCVtvckAFS----IIVSGDAGGNLIIWDLNRAEFvsslsVYKLPIQTIAVNArnaeIAFSTgfycc 2408
Cdd:COG2319   198 ---RTLTGHTGAVRSV----AFSpdgkLLASGSADGTVRLWDLATGKL-----LRTLTGHSGSVRS----VAFSP----- 256

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312211 2409 vvnvNGKILV---KDKLSRIYNENSDENIlcscFYTGANSEWLHK-------NLFITGHPDGIIRIWE 2466
Cdd:COG2319   257 ----DGRLLAsgsADGTVRLWDLATGELL----RTLTGHSGGVNSvafspdgKLLASGSDDGTVRLWD 316
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 1781-1870 3.91e-09

PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.


Pssm-ID: 434260  Cd Length: 99  Bit Score: 56.12  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  1781 VDVNDNSIIDERDPYLQLLHLQSLSSSGKVRRHISkennWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLTILSNTK 1860
Cdd:pfam14844   14 LSITTDHIYFTADDEDEALDSVQESESLGYDKPKH----KRWPISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDTG 89

                           90
                   ....*....|
gi 162312211  1861 NRDSLYQKLV 1870
Cdd:pfam14844   90 TRRKVYRKLV 99
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 2556-2600 1.16e-08

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: 53.30  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162312211 2556 CSLCDSRFSLMEWRSQCRACGNSnVCSDCVS-------MLKDTNIKTCYECY 2600
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRV-FCSKCSSkklplpsFGSGKPVRVCDSCY 52
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 2544-2604 5.46e-07

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: 48.97  E-value: 5.46e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312211   2544 NVHLEKDNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCVS-------MLKDTNIKTCYECYRQMP 2604
Cdd:smart00064    1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRI-FCSKCSSkkaplpkLGIERPVRVCDDCYENLN 67
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 2548-2603 1.01e-05

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: 45.45  E-value: 1.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312211  2548 EKDNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCvSMLKDTNI---------KTCYECYRQM 2603
Cdd:pfam01363    4 VPDSSATVCMICSKPFTFFRRRHHCRNCGRV-FCSAC-SSKKISLLpelgsnkpvRVCDACYDTL 66
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 380-534 3.12e-05

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 46.22  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   380 TLSSPVMPINGYSVSLWLNIESLMNDDGNYAPTTlflisdflKSTLFRLLLDASKKTVVVHIGSSKDTCVVNFSTPITnf 459
Cdd:pfam13385    8 TLPDALLPTSDFTVSAWVKPDSLPGWARAIISSS--------GGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSGASVP-- 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312211   460 fskiykDNpslnppSWHLITLVHRNEksslpNLELYIDGSAVERAACPYPFLSSTLQPLYvslgpsIGSRNQSTP 534
Cdd:pfam13385   78 ------LG------QWTHVAVTYDGG-----TLRLYVNGVLVGSSTLTGGPPPGTGGPLY------IGRSPGGDD 129
DUF4704 pfam15787
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 715-882 4.41e-04

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


Pssm-ID: 464870  Cd Length: 486  Bit Score: 45.35  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   715 GSVTPIIMQSISDAIYNIGGSSILLELV-------------GTAETEAELNFGLQVFFSS-IEDNWRFSENVEQTHSFEI 780
Cdd:pfam15787   13 GGVQLCVTHSIHSILYSVGGIQVLFPLFsqldqpvedeqlpGTSEADYSLCATLLSLIADlLESSPTNQQQMHQLRGFLV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   781 LAQILHSKSHLLVSEETLKIIALMsgvhhTRFKHPLVMNPLLFR----YLILDFDLWSKAPnSNLFVQQLGYIVSLIENN 856
Cdd:pfam15787   93 LGYLLQSASPKHLTLEVLNALLSL-----AKVLVSLPTSEVLLKdlfdHILFNPKLWIYTD-YEVQKKLYSYLATDFVSD 166

                          170       180
                   ....*....|....*....|....*.
gi 162312211   857 DYAGFNVKRLMKMQilkKLLTAMRNC 882
Cdd:pfam15787  167 SRIYTNVRRVSTVQ---RLLDTLKQF 189
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2333-2370 9.96e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 9.96e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 162312211   2333 SLKRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWD 2370
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
Beach smart01026
Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the ...
 1919-2202 6.82e-173

Beige/BEACH domain; The BEACH domain was described in the BEIGE protein (D1035670) and in the highly homologous CHS protein. The BEACH domain is usually followed by a series of WD repeats. The function of the BEACH domain is unknown.


Pssm-ID: 214982  Cd Length: 280  Bit Score: 531.80  E-value: 6.82e-173
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1919 TKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLL 1998
Cdd:smart01026    1 TQKWQNGEISNFEYLMHLNTLAGRSYNDLTQYPVFPWVLADYTSETLDLSNPSTFRDLSKPIGALNPERLEFFYERYEEL 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   1999 LglnDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSKENMADVRELIPEFFYL 2078
Cdd:smart01026   81 E---DPDIPPFHYGTHYSSAGIVLYYLIRLEPFTTLFLQLQGGRFDHADRLFHSVAATWRSASLESMTDVKELIPEFFYL 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   2079 SEMFINGNGFDFGSRQkESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFH 2158
Cdd:smart01026  158 PEFLVNINGFDFGTRQ-DGEDVDDVELPPWAKGSPEEFIRKHREALESEYVSQHLHHWIDLIFGYKQRGKEAVEALNVFH 236

                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....
gi 162312211   2159 HLSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:smart01026  237 PLTYEGAVDLDSIEDPVERKALEGQIHNFGQTPKQLFKEPHPPR 280
Beach pfam02138
Beige/BEACH domain;
1920-2202 1.68e-169

Beige/BEACH domain;


Pssm-ID: 460459  Cd Length: 277  Bit Score: 522.04  E-value: 1.68e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  1920 KRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLLl 1999
Cdd:pfam02138    1 KKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPVFPWVLADYTSEELDLNDPSTYRDLSKPIGALNEERLEKFKERYEEL- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  2000 glnDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSkENMADVRELIPEFFYLS 2079
Cdd:pfam02138   80 ---EDDDPPFHYGSHYSSPGIVLYYLIRLEPFTTLHIELQGGKFDHPDRLFHSIEEAWRSAS-NSTSDVKELIPEFFYLP 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  2080 EMFINGNGFDFGSRQkESTPINDVILPPWAKGDPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFHH 2159
Cdd:pfam02138  156 EFLLNSNNFDLGGRQ-DGEKVDDVELPPWAKKSPEEFVRKHREALESDYVSENLHEWIDLIFGYKQRGEEAVEALNVFHP 234

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 162312211  2160 LSYQGAIDLENIENEFELAAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:pfam02138  235 LTYEGSVDLDSIKDPVERDAIEAQIKNFGQTPKQLFTKPHPPR 277
Beach cd06071
BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in ...
 1919-2202 4.91e-144

BEACH (Beige and Chediak-Higashi) domains, implicated in membrane trafficking, are present in a family of proteins conserved throughout eukaryotes. This group contains human lysosomal trafficking regulator (LYST), LPS-responsive and beige-like anchor (LRBA) and neurobeachin. Disruption of LYST leads to Chediak-Higashi syndrome, characterized by severe immunodeficiency, albinism, poor blood coagulation and neurologic problems. Neurobeachin is a candidate gene linked to autism. LBRA seems to be upregulated in several cancer types. It has been shown that the BEACH domain itself is important for the function of these proteins.


Pssm-ID: 100117 [Multi-domain]  Cd Length: 275  Bit Score: 449.39  E-value: 4.91e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1919 TKRWERREISNFNYLQIVNTLAGRTYNDLTQYPVFPWVIADYTSKELDLNNPKTYRNFCKPMGAQHPERESQFNERYDLl 1998
Cdd:cd06071     1 TKKWQNGEISNFEYLMYLNTLAGRSFNDLSQYPIFPWVISDYTSEELDLNDPSTYRDLSKPIGALNKERLQLLKERYES- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1999 lgLNDSQQQPFHYGTHYSSAMIVCSYLIRLRPFVDSYLALQGGQFDHADRLFYSIEQAWRSSSkENMADVRELIPEFFYL 2078
Cdd:cd06071    80 --DSDDSDPPFHYGSHYSNPAIVLYYLVRLEPFTTLHLSLQGGHFDAADRLFNSIPSSWRSAS-ENPSDVKELIPEFYYL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2079 SEMFINGNGFDFGsrQKESTPINDVILPPWAKGdPAIFVQKNREALESKYVSAHLHEWIDLVFGCKQRGDEAVAATNVFH 2158
Cdd:cd06071   157 PEFFLNINKFDFG--KQDGEKVNDVELPPWAKS-PEEFIRKHREALESEYVSKNLHHWIDLIFGYKQRGEEAVKAKNVFH 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 162312211 2159 HLSYQGAIDLENIENEFElaAAVGIIHNFGQTPKQVFKKPHPQR 2202
Cdd:cd06071   234 PLTYEGSVDLDSIDVERE--AIEAQINNFGQTPVQLFTKPHPKR 275
PH_BEACH cd01201
Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in ...
 1738-1871 4.75e-19

Pleckstrin homology domain in BEACH domain containing proteins; The BEACH domain is present in several eukaroyotic proteins CHS, neurobeachin (Nbea), LRBA (also called BGL, beige-like, or CDC4L), FAN, KIAA1607, and LvsA-LvsF. CHS is a rare, autosomal recessive disorder that can cause severe immunodeficiency and albinism in mammals and beige is the name for the CHS disease in mice. The CHS disease is associated with the presence of giant, perinuclear vesicles (lysosomes, melanosomes, and others) and CHS protein is thought to play an important role in the fusion, fission, or trafficking of these vesicles. All BEACH proteins contain the following domains: PH, BEACH, and WD40. The WD40 domain is involved in mediating protein-protein interactions involved in targeting proteins to subcellular compartments. The combined PH-BEACH motifs may present a single continuous structural unit involved in protein binding. Some members have an additional N-terminal Laminin G-like (LamG) domains Ca++ mediated receptors or an additional C-terminal FYVE zinc-binding domain which targets proteins to membrane lipids via interaction with phosphatidylinositol-3-phosphate, PI3P. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275391  Cd Length: 112  Bit Score: 84.59  E-value: 4.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 1738 DSIQDVYNVSRIFGLEATEGILLLGKQYLYLMDNFFLRSDNEIVDVNDNSIIDERDPYLqllhlqslsssgkvrrhiske 1817
Cdd:cd01201     1 EKILLSVNCSLVTPLDVIEGRLLITKTHLYFVDDFTISEDGKIVVINSQKVLSYKEHLV--------------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162312211 1818 nnWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLtiLS-NTKNRDSLYQKLVA 1871
Cdd:cd01201    60 --FKWSLSDIREVHKRRYLLRDTALEIFFTDGTNYF--LNfPSKERNDVYKKLLS 110
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2255-2466 2.65e-13

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 73.14  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2255 FAADYTPLGPntFLAWGRVDNTVQLIsDQLDKQPVMFEELHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIkas 2333
Cdd:cd00200    13 TCVAFSPDGK--LLATGSGDGTIKVW-DLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDKTIRLWDLETGECV--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2334 lkRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIqtiavnarnaeiafstgfYCCVVNVN 2413
Cdd:cd00200    87 --RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWV------------------NSVAFSPD 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162312211 2414 GKILV---KDKLSRIYNENS----------DENILCSCFYTGANSewlhknlFITGHPDGIIRIWE 2466
Cdd:cd00200   147 GTFVAsssQDGTIKLWDLRTgkcvatltghTGEVNSVAFSPDGEK-------LLSSSSDGTIKLWD 205
WD40 COG2319
WD40 repeat [General function prediction only];
2254-2466 2.28e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 68.40  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2254 AFAADytplgpNTFLAWGRVDNTVQLISDQLDKQPVMFEElHSEKITHV-VACDERTFLTASLDLTLRLWTLSTNKPIka 2332
Cdd:COG2319   127 AFSPD------GKTLASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVaFSPDGKLLASGSDDGTVRLWDLATGKLL-- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2333 slkRVLYGHRYRITCVtvckAFS----IIVSGDAGGNLIIWDLNRAEFvsslsVYKLPIQTIAVNArnaeIAFSTgfycc 2408
Cdd:COG2319   198 ---RTLTGHTGAVRSV----AFSpdgkLLASGSADGTVRLWDLATGKL-----LRTLTGHSGSVRS----VAFSP----- 256

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312211 2409 vvnvNGKILV---KDKLSRIYNENSDENIlcscFYTGANSEWLHK-------NLFITGHPDGIIRIWE 2466
Cdd:COG2319   257 ----DGRLLAsgsADGTVRLWDLATGELL----RTLTGHSGGVNSvafspdgKLLASGSDDGTVRLWD 316
WD40 COG2319
WD40 repeat [General function prediction only];
2254-2466 8.87e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2254 AFAADytplgpNTFLAWGRVDNTVQLISDQLDKQPVMFEElHSEKITHV-VACDERTFLTASLDLTLRLWTLSTNKPIka 2332
Cdd:COG2319   169 AFSPD------GKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVaFSPDGKLLASGSADGTVRLWDLATGKLL-- 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2333 slkRVLYGHRYRITCVtvckAFS----IIVSGDAGGNLIIWDLNRAEFVSSlsvykLPIQTIAVNArnaeIAFSTgfycc 2408
Cdd:COG2319   240 ---RTLTGHSGSVRSV----AFSpdgrLLASGSADGTVRLWDLATGELLRT-----LTGHSGGVNS----VAFSP----- 298

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312211 2409 vvnvNGKILV---KDKLSRIYN----------ENSDENILCSCFytGANSEWLhknlfITGHPDGIIRIWE 2466
Cdd:COG2319   299 ----DGKLLAsgsDDGTVRLWDlatgkllrtlTGHTGAVRSVAF--SPDGKTL-----ASGSDDGTVRLWD 358
WD40 COG2319
WD40 repeat [General function prediction only];
2254-2465 1.08e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2254 AFAADytplgpNTFLAWGRVDNTVQLIsDQLDKQPVMFEELHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIka 2332
Cdd:COG2319   211 AFSPD------GKLLASGSADGTVRLW-DLATGKLLRTLTGHSGSVRSVAFSpDGRLLASGSADGTVRLWDLATGELL-- 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2333 slkRVLYGHRYRITCVtvckAFS----IIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIQTiavnarnaeIAFSTgfycc 2408
Cdd:COG2319   282 ---RTLTGHSGGVNSV----AFSpdgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS---------VAFSP----- 340

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312211 2409 vvnvNGKILV---KDKLSRIYNENSDEnilCSCFYTGaNSEWLHK-------NLFITGHPDGIIRIW 2465
Cdd:COG2319   341 ----DGKTLAsgsDDGTVRLWDLATGE---LLRTLTG-HTGAVTSvafspdgRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2263-2392 1.54e-10

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 64.66  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2263 GPNTFLAWGRVDNTVQLISDQLDKqPVMFEELHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIKaslkrVLYGH 2341
Cdd:cd00200   145 PDGTFVASSSQDGTIKLWDLRTGK-CVATLTGHTGEVNSVAFSpDGEKLLSSSSDGTIKLWDLSTGKCLG-----TLRGH 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 162312211 2342 RYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIQTIAV 2392
Cdd:cd00200   219 ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAW 269
WD40 COG2319
WD40 repeat [General function prediction only];
2264-2466 3.86e-09

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.47  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2264 PNTFLAWGRVDNTVQLISDQLDKQPVMFEELHSEKITHVVACDERTFLTASLDLTLRLWTLSTNKPIkaslkRVLYGHRY 2343
Cdd:COG2319    47 DGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLL-----RTLTGHTG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2344 RITCVtvckAFS----IIVSGDAGGNLIIWDLNRAEFVSSLSVyklpiQTIAVNArnaeIAFSTgfyccvvnvNGKILV- 2418
Cdd:COG2319   122 AVRSV----AFSpdgkTLASGSADGTVRLWDLATGKLLRTLTG-----HSGAVTS----VAFSP---------DGKLLAs 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312211 2419 --KDKLSRIYNENSDENILcscFYTGaNSEWLHK-------NLFITGHPDGIIRIWE 2466
Cdd:COG2319   180 gsDDGTVRLWDLATGKLLR---TLTG-HTGAVRSvafspdgKLLASGSADGTVRLWD 232
PH_BEACH pfam14844
PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the ...
 1781-1870 3.91e-09

PH domain associated with Beige/BEACH; This PH domain is found in proteins containing the Beige/BEACH domain (pfam02138), it immediately precedes the Beige/BEACH domain.


Pssm-ID: 434260  Cd Length: 99  Bit Score: 56.12  E-value: 3.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211  1781 VDVNDNSIIDERDPYLQLLHLQSLSSSGKVRRHISkennWHWDFIDLSLVLKRFYLLRDVGLELFFKDGRSFLTILSNTK 1860
Cdd:pfam14844   14 LSITTDHIYFTADDEDEALDSVQESESLGYDKPKH----KRWPISDIKEVHLRRYLLRDTALEIFLIDRTSLFFNFPDTG 89

                           90
                   ....*....|
gi 162312211  1861 NRDSLYQKLV 1870
Cdd:pfam14844   90 TRRKVYRKLV 99
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2334-2466 6.19e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 59.66  E-value: 6.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2334 LKRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWDLNRAEFVSSLSVYKLPIQTIAVNARNAEIAfSTGFyccvvnvn 2413
Cdd:cd00200     1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLA-SGSS-------- 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312211 2414 gkilvkDKLSRIYNENSDEnilCSCFYTGANSEWL------HKNLFITGHPDGIIRIWE 2466
Cdd:cd00200    72 ------DKTIRLWDLETGE---CVRTLTGHTSYVSsvafspDGRILSSSSRDKTIKVWD 121
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
 2556-2600 1.16e-08

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: 53.30  E-value: 1.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 162312211 2556 CSLCDSRFSLMEWRSQCRACGNSnVCSDCVS-------MLKDTNIKTCYECY 2600
Cdd:cd00065     2 CMLCGKKFSLFRRRHHCRRCGRV-FCSKCSSkklplpsFGSGKPVRVCDSCY 52
WD40 COG2319
WD40 repeat [General function prediction only];
2254-2372 1.58e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 56.46  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211 2254 AFAADytplgpNTFLAWGRVDNTVQLISDQLDKQPVMFEElHSEKITHVVAC-DERTFLTASLDLTLRLWTLSTNKPIka 2332
Cdd:COG2319   295 AFSPD------GKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSpDGKTLASGSDDGTVRLWDLATGELL-- 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 162312211 2333 slkRVLYGHRYRITCVtvckAFS----IIVSGDAGGNLIIWDLN 2372
Cdd:COG2319   366 ---RTLTGHTGAVTSV----AFSpdgrTLASGSADGTVRLWDLA 402
FYVE smart00064
Protein present in Fab1, YOTB, Vac1, and EEA1; The FYVE zinc finger is named after four ...
 2544-2604 5.46e-07

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: 48.97  E-value: 5.46e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162312211   2544 NVHLEKDNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCVS-------MLKDTNIKTCYECYRQMP 2604
Cdd:smart00064    1 RPHWIPDEEVSNCMGCGKEFNLTKRRHHCRNCGRI-FCSKCSSkkaplpkLGIERPVRVCDDCYENLN 67
FYVE pfam01363
FYVE zinc finger; The FYVE zinc finger is named after four proteins that it has been found in: ...
 2548-2603 1.01e-05

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: 45.45  E-value: 1.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312211  2548 EKDNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCvSMLKDTNI---------KTCYECYRQM 2603
Cdd:pfam01363    4 VPDSSATVCMICSKPFTFFRRRHHCRNCGRV-FCSAC-SSKKISLLpelgsnkpvRVCDACYDTL 66
Laminin_G_3 pfam13385
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ...
 380-534 3.12e-05

Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.


Pssm-ID: 463865 [Multi-domain]  Cd Length: 151  Bit Score: 46.22  E-value: 3.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   380 TLSSPVMPINGYSVSLWLNIESLMNDDGNYAPTTlflisdflKSTLFRLLLDASKKTVVVHIGSSKDTCVVNFSTPITnf 459
Cdd:pfam13385    8 TLPDALLPTSDFTVSAWVKPDSLPGWARAIISSS--------GGGGYSLGLDGDGRLRFAVNGGNGGWDTVTSGASVP-- 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 162312211   460 fskiykDNpslnppSWHLITLVHRNEksslpNLELYIDGSAVERAACPYPFLSSTLQPLYvslgpsIGSRNQSTP 534
Cdd:pfam13385   78 ------LG------QWTHVAVTYDGG-----TLRLYVNGVLVGSSTLTGGPPPGTGGPLY------IGRSPGGDD 129
FYVE_endofin cd15729
FYVE domain found in endofin and similar proteins; Endofin, also termed zinc finger FYVE ...
 2550-2600 3.91e-05

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: 43.50  E-value: 3.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312211 2550 DNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCVSM------LKDTNIKTCYECY 2600
Cdd:cd15729    10 DSEAPNCMQCEVKFTFTKRRHHCRACGKV-LCSACCSLkarleyLDNKEARVCVPCY 65
FYVE_ZFY26 cd15724
FYVE domain found in FYVE domain-containing protein 26 (ZFY26 or ZFYVE26); ZFY26, also termed ...
 2550-2600 1.17e-04

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: 42.12  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 162312211 2550 DNTSELCSLCDS-RFSLMEWRSQCRACGNSnVCSDC------VSMLKDTNIKTCYECY 2600
Cdd:cd15724     4 DEAVSVCMVCQVeRFSMFNRRHHCRRCGRV-VCSSCstkkmlVEGYRENPVRVCDQCY 60
FYVE_WDFY3 cd15719
FYVE domain found in WD40 repeat and FYVE domain-containing protein 3 (WDFY3) and similar ...
 2546-2603 1.37e-04

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: 41.99  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 162312211 2546 HLEKDNTSELCSLCDSRFSLMEWRSQCRACGN--SNVCSDCVSMLKDTNI----KTCYECYRQM 2603
Cdd:cd15719     2 HWVKDEGGDSCTGCSVRFSLTERRHHCRNCGQlfCSKCSRFESEIRRLRIsrpvRVCQACYNIL 65
FYVE_PKHF1 cd15754
FYVE domain found in protein containing both PH and FYVE domains 1 (phafin-1) and similar ...
 2550-2603 2.34e-04

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: 41.48  E-value: 2.34e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162312211 2550 DNTSELCSLC-DSRFSLMEWRSQCRACGNSnVCSDC------VSMLKDTNIKTCYECYRQM 2603
Cdd:cd15754     5 DKATDICMRCtQTNFSLLTRRHHCRKCGFV-VCHECsrqrflIPRLSPKPVRVCSLCYRKL 64
FYVE_scVPS27p_like cd15760
FYVE domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 27 ...
 2546-2583 2.57e-04

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: 41.13  E-value: 2.57e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 162312211 2546 HLEKDNTselCSLCDSRFSLMEWRSQCRACGNSnVCSD 2583
Cdd:cd15760     1 HWKPDSR---CDVCRKKFGLFKRRHHCRNCGDS-FCSE 34
FYVE_FGD6 cd15743
FYVE domain found in FYVE, RhoGEF and PH domain-containing protein 6 (FGD6) and similar ...
 2550-2600 3.79e-04

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: 40.50  E-value: 3.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 162312211 2550 DNTSELCSLCDSRFSLMEWRSQCRACGNSnVCSDCVS------MLKDTNIKTCYECY 2600
Cdd:cd15743     6 DSRVTMCMICTSEFTVTWRRHHCRACGKV-VCGSCSSnkapleYLKNKSARVCDECF 61
DUF4704 pfam15787
Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in ...
 715-882 4.41e-04

Neurobeachin/BDCP, DUF4704 alpha solenoid region; This domain of unknown function is found in eukaryotes on neurobeachin and BEACH domain-containing proteins (BDCPs). Mutations in this proteins are associated with Lipopolysaccharide-responsive and beige-like anchor (LRBA) deficiency. According to structure prediction is adopts an alpha-helical solenoid structure.


Pssm-ID: 464870  Cd Length: 486  Bit Score: 45.35  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   715 GSVTPIIMQSISDAIYNIGGSSILLELV-------------GTAETEAELNFGLQVFFSS-IEDNWRFSENVEQTHSFEI 780
Cdd:pfam15787   13 GGVQLCVTHSIHSILYSVGGIQVLFPLFsqldqpvedeqlpGTSEADYSLCATLLSLIADlLESSPTNQQQMHQLRGFLV 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162312211   781 LAQILHSKSHLLVSEETLKIIALMsgvhhTRFKHPLVMNPLLFR----YLILDFDLWSKAPnSNLFVQQLGYIVSLIENN 856
Cdd:pfam15787   93 LGYLLQSASPKHLTLEVLNALLSL-----AKVLVSLPTSEVLLKdlfdHILFNPKLWIYTD-YEVQKKLYSYLATDFVSD 166

                          170       180
                   ....*....|....*....|....*.
gi 162312211   857 DYAGFNVKRLMKMQilkKLLTAMRNC 882
Cdd:pfam15787  167 SRIYTNVRRVSTVQ---RLLDTLKQF 189
FYVE_RBNS5 cd15716
FYVE domain found in FYVE finger-containing Rab5 effector protein rabenosyn-5 (Rbsn-5) and ...
 2550-2600 5.38e-04

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: 40.40  E-value: 5.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 162312211 2550 DNTSELCSLCDSRFSLMEWRSQCRACGnSNVCSDCvSMLKDTNIKTCYECY 2600
Cdd:cd15716     7 DSDVPFCPDCGKKFNLARRRHHCRLCG-SIMCNKC-SQFLPLHIRCCHHCK 55
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 2295-2370 7.34e-04

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 44.25  E-value: 7.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162312211 2295 HSEKITHVVACDERTFLT-ASLDLTLRLWTLSTNKPIKaslkrVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWD 2370
Cdd:cd00200   218 HENGVNSVAFSPDGYLLAsGSEDGTIRVWDLRTGECVQ-----TLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 2333-2370 9.96e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 9.96e-04
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 162312211   2333 SLKRVLYGHRYRITCVTVCKAFSIIVSGDAGGNLIIWD 2370
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
FYVE_ZF21 cd15727
FYVE domain found in zinc finger FYVE domain-containing protein 21 (ZF21) and similar proteins; ...
 2550-2601 6.65e-03

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: 37.36  E-value: 6.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 162312211 2550 DNTSELCSLCDSRFSLMEWRSQCRACGnSNVCSDCVS-------MLKDTNIKTCYECYR 2601
Cdd:cd15727     7 DKECPVCMSCKKKFDFFKRRHHCRRCG-KCFCSDCCSnkvplprMCFVDPVRVCNECAL 64
FYVE_FGD5 cd15742
FYVE-like domain found in FYVE, RhoGEF and PH domain-containing protein 5 (FGD5) and similar ...
 2555-2603 6.73e-03

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: 37.22  E-value: 6.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 162312211 2555 LCSLCDSRFSLMEWRSQCRACGNSnVCSDC------VSMLKDTNIKTCYECYRQM 2603
Cdd:cd15742    11 MCMNCGSDFTLTLRRHHCHACGKI-VCRNCsrnkypLKYLKDRPAKVCDGCFAEL 64
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
 2555-2600 8.16e-03

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: 36.71  E-value: 8.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 162312211 2555 LCSLCDSRFSLMEWRSQCRACGnSNVCSDCVSMLK-----DTNIKT--CYECY 2600
Cdd:cd15745     1 ACAICAKAFSLFRRKYVCRLCG-GVVCHSCSSEDLvlsvpDTCIYLrvCKTCY 52
 
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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