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Conserved domains on  [gi|1034602410|ref|XP_016880940|]
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pleckstrin homology domain-containing family M member 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-RING_9 pfam13901
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ...
 846-1048 1.26e-98

Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169


:

Pssm-ID: 464030  Cd Length: 205  Bit Score: 309.55  E-value: 1.26e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  846 KLCAFSGLYYCDICHQDDASVIPARIIHNWDLTKRPICRQALKFLTQIRAQPLINLQMVNASLYEHVERMHLIGRRREQL 925
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  926 KLLGDYLGLCRSGALKELSK--RLNHRNYLLESPHRFSVADLQQIADGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 1003
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034602410 1004 CQHHDIIFPFEFDTTVRCAECKTVFHQSCQAVVKKGCPRCARRRK 1048
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 18-188 3.00e-82

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


:

Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 264.45  E-value: 3.00e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   18 IKKKLVGSVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKHIRAEAGGKRKKSAhqkPLPQPVFWPLLKAVT 97
Cdd:cd17679      4 LTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   98 HKHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFE 177
Cdd:cd17679     81 HRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFE 160

                          170
                   ....*....|.
gi 1034602410  178 LSYKSAILNEW 188
Cdd:cd17679    161 LPYNSSLLNTW 171
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 499-629 3.07e-78

Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; PLEKHM1 is thought to function in vesicular transport in osteoclasts. Mutations in the PLEKHM1 gene are associated with osteopetrosis OPTB6. PLEKHM1 contains an N-terminal RUN domain (RPIP8/RaP2 interacting protein 8, UNC-14 and NESCA/new molecule containing SH3 at the carboxyl-terminus), followed by a PH domain, and either a C1 domain or a DUF4206 domain at its C-terminus. The RUN domain is thought to be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. 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: 241475  Cd Length: 132  Bit Score: 251.68  E-value: 3.07e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  499 VPSPGRRqaqAAPSQGHKSFRVVHRRQMGLSNPFRGLMKLGTVERRGAMGIWKELFCELSPLEFRLYLSNEEHTCVENCS 578
Cdd:cd13321      5 APSQGPL---SEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCS 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034602410  579 LLRCESVGPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 629
Cdd:cd13321     82 LLRCESVGPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 685-777 3.93e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 40.61  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   685 IKESLLYLYMD---RTWMPYIFSLSLEALKCFRIRNNEK--------MLSDShgveTIRDILPDTSLGGPSFFKIITA-K 752
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 1034602410   753 AVLKLQAGNAEEAALWRDLVRKVLA 777
Cdd:smart00233   78 KTLLLQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
zf-RING_9 pfam13901
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ...
 846-1048 1.26e-98

Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169


Pssm-ID: 464030  Cd Length: 205  Bit Score: 309.55  E-value: 1.26e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  846 KLCAFSGLYYCDICHQDDASVIPARIIHNWDLTKRPICRQALKFLTQIRAQPLINLQMVNASLYEHVERMHLIGRRREQL 925
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  926 KLLGDYLGLCRSGALKELSK--RLNHRNYLLESPHRFSVADLQQIADGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 1003
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034602410 1004 CQHHDIIFPFEFDTTVRCAECKTVFHQSCQAVVKKGCPRCARRRK 1048
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 18-188 3.00e-82

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 264.45  E-value: 3.00e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   18 IKKKLVGSVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKHIRAEAGGKRKKSAhqkPLPQPVFWPLLKAVT 97
Cdd:cd17679      4 LTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   98 HKHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFE 177
Cdd:cd17679     81 HRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFE 160

                          170
                   ....*....|.
gi 1034602410  178 LSYKSAILNEW 188
Cdd:cd17679    161 LPYNSSLLNTW 171
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 499-629 3.07e-78

Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; PLEKHM1 is thought to function in vesicular transport in osteoclasts. Mutations in the PLEKHM1 gene are associated with osteopetrosis OPTB6. PLEKHM1 contains an N-terminal RUN domain (RPIP8/RaP2 interacting protein 8, UNC-14 and NESCA/new molecule containing SH3 at the carboxyl-terminus), followed by a PH domain, and either a C1 domain or a DUF4206 domain at its C-terminus. The RUN domain is thought to be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. 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: 241475  Cd Length: 132  Bit Score: 251.68  E-value: 3.07e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  499 VPSPGRRqaqAAPSQGHKSFRVVHRRQMGLSNPFRGLMKLGTVERRGAMGIWKELFCELSPLEFRLYLSNEEHTCVENCS 578
Cdd:cd13321      5 APSQGPL---SEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCS 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034602410  579 LLRCESVGPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 629
Cdd:cd13321     82 LLRCESVGPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 49-182 5.02e-36

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 132.78  E-value: 5.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   49 TMCSALEAVFIHGLHAKHIRAEAGGKRKksahqkplPQPVFWPLLKAVT-----HKHIISELEHLTFVNT---DVGRCRA 120
Cdd:pfam02759    1 QLCAALEALLSHGLKRSSLLILRAAGLL--------PERSFWALLERVGklvppAEELLSSVQELEQIHTpysPDGRGRA 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034602410  121 WLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFELSYKS 182
Cdd:pfam02759   73 WIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
118-181 7.78e-19

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 81.12  E-value: 7.78e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034602410   118 CRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFELSYK 181
Cdd:smart00593    1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 987-1040 3.91e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 44.77  E-value: 3.91e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034602410   987 HVYHCDLCTQRGFiCQICQHHDIIFpfeFDTTVRCAECKTVFHQSCQAVVKKGC 1040
Cdd:smart00109    1 HKHVFRTFTKPTF-CCVCRKSIWGS---FKQGLRCSECKVKCHKKCADKVPKAC 50
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 535-625 4.81e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.31  E-value: 4.81e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   535 LMKLGTVERRGAMGI--WKELFCELSPLEFRLYLSNEEHTC--------VENCSLLRCESVGPAHSDGRFELVFS-GKKL 603
Cdd:smart00233    1 VIKEGWLYKKSGGGKksWKKRYFVLFNSTLLYYKSKKDKKSykpkgsidLSGCTVREAPDPDSSKKPHCFEIKTSdRKTL 80

                            90       100
                    ....*....|....*....|..
gi 1034602410   604 ALRASSQDEAEDWLDRVREALQ 625
Cdd:smart00233   81 LLQAESEEEREKWVEALRKAIA 102
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 685-777 3.93e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 40.61  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   685 IKESLLYLYMD---RTWMPYIFSLSLEALKCFRIRNNEK--------MLSDShgveTIRDILPDTSLGGPSFFKIITA-K 752
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 1034602410   753 AVLKLQAGNAEEAALWRDLVRKVLA 777
Cdd:smart00233   78 KTLLLQAESEEEREKWVEALRKAIA 102
 
Name Accession Description Interval E-value
zf-RING_9 pfam13901
Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members ...
 846-1048 1.26e-98

Putative zinc-RING and/or ribbon; This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain, pfam00169


Pssm-ID: 464030  Cd Length: 205  Bit Score: 309.55  E-value: 1.26e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  846 KLCAFSGLYYCDICHQDDASVIPARIIHNWDLTKRPICRQALKFLTQIRAQPLINLQMVNASLYEHVERMHLIGRRREQL 925
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  926 KLLGDYLGLCRSGALKELSK--RLNHRNYLLESPHRFSVADLQQIADGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 1003
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1034602410 1004 CQHHDIIFPFEFDTTVRCAECKTVFHQSCQAVVKKGCPRCARRRK 1048
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 18-188 3.00e-82

RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and similar proteins; PLEKHM1, also called PH domain-containing family M member 1, or 162 kDa adapter protein (AP162), may act as a multivalent adapter protein that regulates Rab7-dependent and HOPS complex-dependent fusion events in the endolysosomal system and couples autophagic and the endocytic trafficking pathways. This model represents the RUN domain of PLEKHM1.


Pssm-ID: 439041 [Multi-domain]  Cd Length: 171  Bit Score: 264.45  E-value: 3.00e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   18 IKKKLVGSVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKHIRAEAGGKRKKSAhqkPLPQPVFWPLLKAVT 97
Cdd:cd17679      4 LTKELSSSVKELQLEYVSSDEVVTSSDDGANTLCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   98 HKHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFE 177
Cdd:cd17679     81 HRDVIDQIEHLSQITTDVGRCRAWIRLALNDGLLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFE 160

                          170
                   ....*....|.
gi 1034602410  178 LSYKSAILNEW 188
Cdd:cd17679    161 LPYNSSLLNTW 171
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 499-629 3.07e-78

Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; PLEKHM1 is thought to function in vesicular transport in osteoclasts. Mutations in the PLEKHM1 gene are associated with osteopetrosis OPTB6. PLEKHM1 contains an N-terminal RUN domain (RPIP8/RaP2 interacting protein 8, UNC-14 and NESCA/new molecule containing SH3 at the carboxyl-terminus), followed by a PH domain, and either a C1 domain or a DUF4206 domain at its C-terminus. The RUN domain is thought to be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. 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: 241475  Cd Length: 132  Bit Score: 251.68  E-value: 3.07e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  499 VPSPGRRqaqAAPSQGHKSFRVVHRRQMGLSNPFRGLMKLGTVERRGAMGIWKELFCELSPLEFRLYLSNEEHTCVENCS 578
Cdd:cd13321      5 APSQGPL---SEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCS 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034602410  579 LLRCESVGPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 629
Cdd:cd13321     82 LLRCESVGPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 49-182 5.02e-36

RUN domain; This domain is present in several proteins that are linked to the functions of GTPases in the Rap and Rab families. They could hence play important roles in multiple Ras-like GTPase signalling pathways. The domain is comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases.


Pssm-ID: 460679  Cd Length: 134  Bit Score: 132.78  E-value: 5.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   49 TMCSALEAVFIHGLHAKHIRAEAGGKRKksahqkplPQPVFWPLLKAVT-----HKHIISELEHLTFVNT---DVGRCRA 120
Cdd:pfam02759    1 QLCAALEALLSHGLKRSSLLILRAAGLL--------PERSFWALLERVGklvppAEELLSSVQELEQIHTpysPDGRGRA 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034602410  121 WLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFELSYKS 182
Cdd:pfam02759   73 WIRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 24-178 4.46e-34

RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new molecule containing SH3 at the carboxyl-terminus), is a less conserved protein motif that comprises six conserved regions, which in some proteins have considerable insertions between them. The domain core is thought to take up a predominantly alpha fold, with basic amino acids in regions A and D possibly playing a functional role in interactions with Ras GTPases. RUN domains are often found in proteins linked particularly to the functions of GTPases in the Rap and Rab families, suggesting the RUN domain may be involved in Rab-mediated membrane trafficking, possibly as a Rab-binding site. RUN domain-containing proteins could hence play important roles in multiple Ras-like GTPase signalling pathways.


Pssm-ID: 439038  Cd Length: 154  Bit Score: 127.93  E-value: 4.46e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   24 GSVKALQKQYVSLDTV-------VTSEDGDANTMCSALEAVFIHGLHAKHIRAEaggkrkksahqkplpQPVFWPLLKAV 96
Cdd:cd17671      1 KAVKELLESFADNGEAddsaaltLTDDDPVVGRLCAALEAILSHGLKPKRFGGG---------------KVSFWDFLEAL 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   97 TH-------KHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQ 169
Cdd:cd17671     66 EKllpapslKQAIRDINSLSNVKTDDGRGRAWIRLALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLV 145


                   ....*....
gi 1034602410  170 GLTSLSFEL 178
Cdd:cd17671    146 GLSSLDFNL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 21-179 6.32e-31

RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN domain-containing protein 2A (RUNDC2A), belongs to the sorting nexin family. Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain, a phospholipid-binding motif, or through protein-protein interactions with membrane-associated protein complexes. Some sorting nexin family members have been shown to facilitate protein sorting. This model contains the RUN domain of SNX29.


Pssm-ID: 439051  Cd Length: 166  Bit Score: 119.64  E-value: 6.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   21 KLVGSVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGL-----HAKHIRAEAGGKRKKSAHQKPLPQPVFWPLLKA 95
Cdd:cd17689      1 RLLDAVKQCQIRFGGKTELATESDSRVSCLCAQLEAVLQHGLktsrsPNLVSSAVTQVSGLAGSLGSAETEPTFWPFVKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   96 VTHKHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLS 175
Cdd:cd17689     81 HLTKHELERFELLKNIWTDIGRGRAWLRSALNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSIL 160


                   ....
gi 1034602410  176 FELS 179
Cdd:cd17689    161 FALS 164
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 17-178 6.28e-26

RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and similar proteins; PLEKHM2, also called PH domain-containing family M member 2, or Salmonella-induced filaments A (SifA) and Kinesin-Interacting Protein (SKIP), is the lysosome, melanosome and lytic granule cargo adaptor that controls lysosome positioning using a composite kinesin-1 heavy and light chain-binding domain. In addition to kinesin-1, it also interacts with several Rabs to affect endosomal trafficking. This model represents the RUN domain of PLEKHM2.


Pssm-ID: 439042  Cd Length: 145  Bit Score: 104.25  E-value: 6.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   17 VIKKKLVGSVKALQKQYVSLDT---VVTSEDGDANTMCSALEAVFIHGLhaKHiraeaggkrkksahqkplPQPVFWPLL 93
Cdd:cd17680      1 RILRNISEAIKSLQSYSSSQEEedvLITNENRELQRLCEALDHALLHGL--RR------------------GNRGYWPFV 60

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   94 KAVTHKHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTS 173
Cdd:cd17680     61 KEFTHKETIKQIENLPNVTTDLGRGRAWLYLALNEGSLESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGLEF 140


                   ....*
gi 1034602410  174 LSFEL 178
Cdd:cd17680    141 VQFDL 145
RUN smart00593
domain involved in Ras-like GTPase signaling;
118-181 7.78e-19

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 81.12  E-value: 7.78e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034602410   118 CRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFELSYK 181
Cdd:smart00593    1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 25-178 6.33e-15

RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar proteins; This family includes RUN and FYVE domain-containing protein RUFY1, RUFY2, and RUFY3. RUFY1, also called 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 homolog 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 called 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. RUFY3, also called 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. RUFY1, RUFY2, and RUFY3 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439043  Cd Length: 155  Bit Score: 73.37  E-value: 6.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   25 SVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKhiraeaggKRKKSahqkplPQPVFWPLLKAVTH-----K 99
Cdd:cd17681     12 SIKELIESALSFGRTLDSDHVPLQQFFVILEHVLRHGLKVK--------KSFLG------PNKSFWPVLEHVEKlvpeaN 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034602410  100 HIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDaEEGEFLLSFLQGLTSLSFEL 178
Cdd:cd17681     78 EITASVRDLPGIKTPLGRARAWLRLALMQKKLADYFRALIENKDLLSEFYEPGALMMS-EEAVVIAGLLVGLNVIDCNL 155
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 50-174 1.06e-10

RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 has been characterized as Rab6-interacting protein which is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. It functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. DENND5 has two isoforms, DENND5A and DENND5B. This model represents the first RUN domain of DENND5.


Pssm-ID: 439039  Cd Length: 183  Bit Score: 61.65  E-value: 1.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   50 MCSALEAVFIHGLHAK--------HIRAEAGGKRKksahQKPLPQPVFWPLlkavthKHIISELEhltfVNTDVGRCRAW 121
Cdd:cd17677     55 LCDLLERIWSHGLQTKqgksalwsHLLAYQENEER----LKPLPESLLFDM------KNVQNMKE----IKTDVGYARAW 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034602410  122 LRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEfllSFLQGLTSL 174
Cdd:cd17677    121 IRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRCEDERE---QFLYHLLSL 170
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 49-176 1.36e-10

RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, also called Rab6-interacting protein 1 (Rab6IP1)-like protein, functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5B.


Pssm-ID: 439053 [Multi-domain]  Cd Length: 206  Bit Score: 61.99  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   49 TMCSALEAVFIHGLHAKHIRA-------EAGGKRKKSAHQKPLP-----------QPVFWPLLKAvthkHIISELEH--- 107
Cdd:cd17691     54 SLCDLLERIWSHGLQVKQGKSalwshllHFQEREEKQEHVAESPvanglerrkseTGVNLPTLRV----SLIQDMRHiqn 129

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034602410  108 LTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSF 176
Cdd:cd17691    130 MSEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAFLRCEEEKEQFLYHLLSLNAVDY 198
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 50-178 5.58e-10

RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil domain-containing protein 1 (FYCO1), and similar proteins; The family includes RUFY4 and FYCO1. RUFY4 acts as a positive regulator that enhances autophagy and lysosome tethering in response to Interleukin-4. It is expressed in a cell-specific manner or under specific immunological conditions associated with IL4 expression such as allergic asthma. FYCO1, also called zinc finger FYVE domain-containing protein 7 (ZFYVE7), is a multidomain autophagy adaptor protein that interacts with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7, and phosphatidylinositol 3-phosphate (PI3P), to mediate microtubule plus-end-directed autophagosome transport. Both RUFY4 and FYCO1 contain an N-terminal RUN domain and a C-terminal FYVE domain with two coiled-coil domains in-between; this model represents the RUN domain.


Pssm-ID: 439044  Cd Length: 150  Bit Score: 58.78  E-value: 5.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   50 MCSALEAVFIHGLHAKHIraeaGGKRKKSahqkplpqpvFWPLLKAVTHK---------HIISELEHLTFVNTDVGRCRA 120
Cdd:cd17682     27 FCETLEKILRKGLKEKVS----LGGRRKD----------YWDWLEELLKKlnkipkslsDAVKFVKSCKKVKTNQGRGRL 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034602410  121 WLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDAEEGEFLLSFLQGLTSLSFEL 178
Cdd:cd17682     93 FIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 25-178 1.98e-09

RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 contains two isoforms, RUNDC3A and RUNDC3B. RUNDC3A, also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. RUNDC3B, also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. Both RUNDC3A and RUNDC3B contain a RUN domain.


Pssm-ID: 439046  Cd Length: 150  Bit Score: 57.41  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   25 SVKALQKQYvSLDTVVTSEDgDANTMCSALEAVFIHGLHAKhiraeaggkRKKSAHQKPLPqpvFWPLLKaVTHKHI--- 101
Cdd:cd17684      9 SVKSLIDKA-CLETIDDSSE-ELINFAAILEQILSHRLKPV---------KPWYGSEEPRT---FWDYIR-VACKKVpqn 73

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034602410  102 -ISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRdAEEGEFLLSFLQGLTSLSFEL 178
Cdd:cd17684     74 cIASIEQMENIKSPKAKGRAWIRVALMEKRLSEYLSTALKQTRLTRNFYQDGAIML-SEDATVLCGMLIGLNAIDFSF 150
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 49-167 1.63e-08

RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, also called Rab6-interacting protein 1 (Rab6IP1), is present predominantly in developing neuronal tissue, and functions in membrane trafficking at a crossroads between the Golgi and the endosomal system. It is composed of an N-terminal DENN (Differentially Expressed in Normal and Neoplastic cells) domain followed by two RUN (RPIP8 [RaP2-interacting protein 8], UNC-14, and NESCA [new molecule containing SH3 at the carboxyl terminus]) domains flanking a PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain. This model represents the first RUN domain of DENND5A.


Pssm-ID: 439052 [Multi-domain]  Cd Length: 209  Bit Score: 56.17  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   49 TMCSALEAVFIHGLHAK--------HIRAEAGGKRKK--------------SAHQKPLPQPVFWPLLKAVTH--KHIise 104
Cdd:cd17690     54 SLCDLLERIWSHGLQVKqgksalwsHLLHYQENRERKttssglstsgiildSERRKSDASLAMPPLKISLIQdmRHI--- 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034602410  105 lEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLR-DAEEGEF---LLSF 167
Cdd:cd17690    131 -QNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFLRcDDEKEQFlyhLLSF 196
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 25-178 7.40e-08

RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; RUFY1, also called 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 homolog 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; this model represents the RUN domain.


Pssm-ID: 439056  Cd Length: 156  Bit Score: 52.99  E-value: 7.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   25 SVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLhakhiraeaggKRKKS--AHQKPlpqpvFWPLLKAVTH---- 98
Cdd:cd17694     12 SIKVLIQSALSLGRTLDSDYPPLQQFFVVLEHCLKHGL-----------KVKKSfiGQNKS-----FFGPLELVEKlcpe 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   99 -KHIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDaEEGEFLLSFLQGLTSLSFE 177
Cdd:cd17694     76 aSDIATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMME-EEGAVIVGLLVGLNVIDAN 154


                   .
gi 1034602410  178 L 178
Cdd:cd17694    155 L 155
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 25-178 1.36e-07

RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; RUFY3, also called 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. This model represents the RUN domain of RUFY3.


Pssm-ID: 439058  Cd Length: 156  Bit Score: 52.31  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   25 SVKALQKQYVSLDTVVTSEDGDANTMCSALEAVFIHGLHAKHIRAeagGKRKKsahqkplpqpvFWPLLKAVTH-----K 99
Cdd:cd17696     12 SIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFL---GQNKS-----------FWGPLELVEKlvpeaA 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034602410  100 HIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDaEEGEFLLSFLQGLTSLSFEL 178
Cdd:cd17696     78 EITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMME-EEGAIIAGLLVGLNVIDANF 155
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 101-178 1.43e-07

RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; RUFY2, also called 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. This model represents the RUN domain of RUFY2.


Pssm-ID: 439057  Cd Length: 156  Bit Score: 51.90  E-value: 1.43e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034602410  101 IISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRDaEEGEFLLSFLQGLTSLSFEL 178
Cdd:cd17695     79 IAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMME-EEGAVIVGLLVGLNVIDANL 155
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 987-1040 3.91e-06

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 44.77  E-value: 3.91e-06
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1034602410   987 HVYHCDLCTQRGFiCQICQHHDIIFpfeFDTTVRCAECKTVFHQSCQAVVKKGC 1040
Cdd:smart00109    1 HKHVFRTFTKPTF-CCVCRKSIWGS---FKQGLRCSECKVKCHKKCADKVPKAC 50
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 86-176 3.70e-05

RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN domain-containing protein 3A (RUNDC3A), also called Rap2-interacting protein 8 (RPIP8), may act as an effector of Rap2A GTPase in neuronal cells. It contains a RUN domain.


Pssm-ID: 439061  Cd Length: 151  Bit Score: 45.02  E-value: 3.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   86 QPVFWPLLKAVTHK---HIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTA-LLRdaEEG 161
Cdd:cd17699     56 QRGFWDYIRLACSKvpnNCISSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAiMLR--EES 133

                           90
                   ....*....|....*
gi 1034602410  162 EFLLSFLQGLTSLSF 176
Cdd:cd17699    134 TVLTGMLIGLSAIDF 148
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 535-625 4.81e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.31  E-value: 4.81e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   535 LMKLGTVERRGAMGI--WKELFCELSPLEFRLYLSNEEHTC--------VENCSLLRCESVGPAHSDGRFELVFS-GKKL 603
Cdd:smart00233    1 VIKEGWLYKKSGGGKksWKKRYFVLFNSTLLYYKSKKDKKSykpkgsidLSGCTVREAPDPDSSKKPHCFEIKTSdRKTL 80

                            90       100
                    ....*....|....*....|..
gi 1034602410   604 ALRASSQDEAEDWLDRVREALQ 625
Cdd:smart00233   81 LLQAESEEEREKWVEALRKAIA 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 539-620 7.60e-05

Pleckstrin homology (PH) domain; 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: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 42.53  E-value: 7.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  539 GTVERRGA--MGIWKELFCELSplEFRLYLSNEEH----TCVENCSLLRCESVGPAHSDGR---FELVFS-GKKLALRAS 608
Cdd:cd00821      3 GYLLKRGGggLKSWKKRWFVLF--EGVLLYYKSKKdssyKPKGSIPLSGILEVEEVSPKERphcFELVTPdGRTYYLQAD 80

                           90
                   ....*....|..
gi 1034602410  609 SQDEAEDWLDRV 620
Cdd:cd00821     81 SEEERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 685-777 3.93e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 40.61  E-value: 3.93e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   685 IKESLLYLYMD---RTWMPYIFSLSLEALKCFRIRNNEK--------MLSDShgveTIRDILPDTSLGGPSFFKIITA-K 752
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 1034602410   753 AVLKLQAGNAEEAALWRDLVRKVLA 777
Cdd:smart00233   78 KTLLLQAESEEEREKWVEALRKAIA 102
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 89-176 4.56e-04

RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN domain-containing protein 3B (RUNDC3B), also called Rap2-binding protein 9, or Rap2-interacting protein 9 (RPIP-9), contains a RUN domain in its N-terminal region that mediates interaction with Rap2, an important component of the Mitogen-Activated Protein Kinase (MAPK) cascade, which regulates cellular proliferation and differentiation. It also contains characteristic binding sites for MAPK intermediates. RUNDC3B contains a RUN domain.


Pssm-ID: 439062  Cd Length: 151  Bit Score: 41.88  E-value: 4.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410   89 FWPLLKAVTHK---HIISELEHLTFVNTDVGRCRAWLRLALNDGLMECYLKLLLQEQARLHEYYQPTALLRdAEEGEFLL 165
Cdd:cd17700     59 FWDYIRVACSKvphNCICSIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVL-GEEANMLA 137

                           90
                   ....*....|.
gi 1034602410  166 SFLQGLTSLSF 176
Cdd:cd17700    138 GMLLGLNAIDF 148
PH1_ARAP cd13253
ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, ...
 535-631 5.85e-03

ArfGAP with RhoGAP domain, ankyrin repeat and PH domain Pleckstrin homology (PH) domain, repeat 1; ARAP proteins (also called centaurin delta) are phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating proteins that modulate actin cytoskeleton remodeling by regulating ARF and RHO family members. They bind phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding. There are 3 mammalian ARAP proteins: ARAP1, ARAP2, and ARAP3. All ARAP proteins contain a N-terminal SAM (sterile alpha motif) domain, 5 PH domains, an ArfGAP domain, 2 ankyrin domain, A RhoGap domain, and a Ras-associating domain. This hierarchy contains the first PH domain in ARAP. 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: 270073  Cd Length: 94  Bit Score: 37.37  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034602410  535 LMKLGTverRGAMGIWKELFCELSPLEFRLYLSNEEHTCVENCSLlRCESVGPAHSDGRFELVFSGKKLALRASSQDEAE 614
Cdd:cd13253      6 LDKQGG---QGNNKGFQKRWVVFDGLSLRYFDSEKDAYSKRIIPL-SAISTVRAVGDNKFELVTTNRTFVFRAESDDERN 81

                           90
                   ....*....|....*..
gi 1034602410  615 DWLdrvrEALQKVRPQQ 631
Cdd:cd13253     82 LWC----STLQAAISEY 94
 
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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