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Conserved domains on  [gi|564374726|ref|XP_006247589|]
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pleckstrin homology domain-containing family M member 1 isoform X2 [Rattus norvegicus]

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 ...
 801-1003 1.54e-97

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: 306.08  E-value: 1.54e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   801 KLCAFSGLYYCDFCHQDDASVIPARIIHNWDLTKRPVCRQALKFLAQIRAQPLINLQLVNASLYEHVERMHLIGRSREQL 880
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   881 KLLGDYLGLCRSGALKELSK--RLSHRNYLLESPHKFSVADLQQIAEGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 958
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564374726   959 CHHQDIIFPFEFDTTVRCAECRTVFHQSCQAVVRKGCPRCARRRK 1003
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 460-583 9.62e-79

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: 252.84  E-value: 9.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  460 APSPAVTQDHKNFCVVHRRQMGLSNPFRGLMKLGTVARRGAMGIWKEFFCELSPLELRLYLSDEERTCVESCSLLRCEAV 539
Cdd:cd13321     9 GPLSEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCSLLRCESV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564374726  540 GPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 583
Cdd:cd13321    89 GPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 1-139 6.40e-69

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: 227.47  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKYIRAEAGGKRKKHThqkPLPQPVFWPLLKAVTHKHIISDLEHLVFINTDVGRCRAWLRLALNDG 80
Cdd:cd17679    36 LCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDG 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374726   81 LMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKSAILNEW 139
Cdd:cd17679   113 LLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFELPYNSSLLNTW 171
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 640-732 7.95e-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: 39.84  E-value: 7.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    640 IKESLLYLYAD---RTWIPYIFSLSLESLKCFRVRNNEK--------MLSDShgveTIRDILPDTSLGGPAFFKIITA-K 707
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 564374726    708 AVLKLQAKNTEEAAHWRDLVRKVLA 732
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 ...
 801-1003 1.54e-97

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: 306.08  E-value: 1.54e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   801 KLCAFSGLYYCDFCHQDDASVIPARIIHNWDLTKRPVCRQALKFLAQIRAQPLINLQLVNASLYEHVERMHLIGRSREQL 880
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   881 KLLGDYLGLCRSGALKELSK--RLSHRNYLLESPHKFSVADLQQIAEGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 958
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564374726   959 CHHQDIIFPFEFDTTVRCAECRTVFHQSCQAVVRKGCPRCARRRK 1003
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 460-583 9.62e-79

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: 252.84  E-value: 9.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  460 APSPAVTQDHKNFCVVHRRQMGLSNPFRGLMKLGTVARRGAMGIWKEFFCELSPLELRLYLSDEERTCVESCSLLRCEAV 539
Cdd:cd13321     9 GPLSEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCSLLRCESV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564374726  540 GPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 583
Cdd:cd13321    89 GPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 1-139 6.40e-69

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: 227.47  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKYIRAEAGGKRKKHThqkPLPQPVFWPLLKAVTHKHIISDLEHLVFINTDVGRCRAWLRLALNDG 80
Cdd:cd17679    36 LCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDG 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374726   81 LMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKSAILNEW 139
Cdd:cd17679   113 LLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFELPYNSSLLNTW 171
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 1-133 1.40e-35

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: 131.63  E-value: 1.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726     1 MCSALEAVFIHGLHAKYIRAEAGGKRKkhthqkplPQPVFWPLLKAVT-----HKHIISDLEHLVFINT---DVGRCRAW 72
Cdd:pfam02759    2 LCAALEALLSHGLKRSSLLILRAAGLL--------PERSFWALLERVGklvppAEELLSSVQELEQIHTpysPDGRGRAW 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564374726    73 LRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKS 133
Cdd:pfam02759   74 IRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN smart00593
domain involved in Ras-like GTPase signaling;
69-132 1.17e-16

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 74.96  E-value: 1.17e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564374726     69 CRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYK 132
Cdd:smart00593    1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 489-579 6.95e-06

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: 45.62  E-value: 6.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    489 LMKLGTVARRGamgiWKEFFCELSPLELRLYLSDEER---TCVESCSLLRCEAVGPAHSDGR-----FELVFS-GKKLAL 559
Cdd:smart00233    7 LYKKSGGGKKS----WKKRYFVLFNSTLLYYKSKKDKksyKPKGSIDLSGCTVREAPDPDSSkkphcFEIKTSdRKTLLL 82

                            90       100
                    ....*....|....*....|
gi 564374726    560 RASSQDEAEDWLDRVREALQ 579
Cdd:smart00233   83 QAESEEEREKWVEALRKAIA 102
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 942-995 5.41e-05

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: 41.68  E-value: 5.41e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564374726    942 HVYHCDLCTQRGFiCQICHHQDIIFpfeFDTTVRCAECRTVFHQSCQAVVRKGC 995
Cdd:smart00109    1 HKHVFRTFTKPTF-CCVCRKSIWGS---FKQGLRCSECKVKCHKKCADKVPKAC 50
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 640-732 7.95e-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: 39.84  E-value: 7.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    640 IKESLLYLYAD---RTWIPYIFSLSLESLKCFRVRNNEK--------MLSDShgveTIRDILPDTSLGGPAFFKIITA-K 707
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 564374726    708 AVLKLQAKNTEEAAHWRDLVRKVLA 732
Cdd:smart00233   78 KTLLLQAESEEEREKWVEALRKAIA 102
PH_GAP1-like cd01244
RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; ...
 658-733 3.54e-03

RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; RASAL1, GAP1(m), GAP1(IP4BP), and CAPRI are all members of the GAP1 family of GTPase-activating proteins. They contain N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. They act as a suppressor of RAS enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. PH domains share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 269950  Cd Length: 107  Bit Score: 38.04  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  658 FSLSLESLKCFRVRNNEKM----LSDSHGVETIRDilpdTSLGGPAFFKIITAKAVLKLQAKNTEEAAHWRDLVRKVLAS 733
Cdd:cd01244    26 FRLTNEALSYSKSKGKQPLcsipLEDILAVERVEE----ESFKMKNMFQIVQPDRTLYLQAKNVVELNEWLSALRKVCLC 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 489-578 5.27e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   489 LMKLGTVARRGamgiWKEFFCELSPLELRLYLSDEERTC--------VESCSLLRCEAVGPAHSDGRFELVFS----GKK 556
Cdd:pfam00169    7 LLKKGGGKKKS----WKKRYFVLFDGSLLYYKDDKSGKSkepkgsisLSGCEVVEVVASDSPKRKFCFELRTGertgKRT 82

                           90       100
                   ....*....|....*....|..
gi 564374726   557 LALRASSQDEAEDWLDRVREAL 578
Cdd:pfam00169   83 YLLQAESEEERKDWIKAIQSAI 104
 
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 ...
 801-1003 1.54e-97

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: 306.08  E-value: 1.54e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   801 KLCAFSGLYYCDFCHQDDASVIPARIIHNWDLTKRPVCRQALKFLAQIRAQPLINLQLVNASLYEHVERMHLIGRSREQL 880
Cdd:pfam13901    1 RLCDYTGKYYCSGCHWNDTSVIPARILHNWDFKKYPVSKFAKQLLDSIYSQPLLNLSDLNPSLYSKVKELAKVRELREQL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   881 KLLGDYLGLCRSGALKELSK--RLSHRNYLLESPHKFSVADLQQIAEGVYEGFLKALIEFASQHVYHCDLCTQRGFICQI 958
Cdd:pfam13901   81 KLLKDYLKTCRFAAEEELLKlfRLRPRHHLLEDSHLYSLQDLVDIKNGSLLPFLEELVQFAEKHVTNCELCQGKGFICEL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 564374726   959 CHHQDIIFPFEFDTTVRCAECRTVFHQSCQAVVRKGCPRCARRRK 1003
Cdd:pfam13901  161 CNSDDIIFPFDIDTTSRCEKCKAVFHKSCFRSGASPCPKCERLQK 205
PH_PLEKHM1 cd13321
Pleckstrin homology domain-containing family M member 1 Pleckstrin homology (PH) domain; ...
 460-583 9.62e-79

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: 252.84  E-value: 9.62e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  460 APSPAVTQDHKNFCVVHRRQMGLSNPFRGLMKLGTVARRGAMGIWKEFFCELSPLELRLYLSDEERTCVESCSLLRCEAV 539
Cdd:cd13321     9 GPLSEPSQVQKPFSVVHRRQMGLSNPFRGLLKLGTLERRGAMGIWKEFYCELSPLEFRLYLSAEERVCVENCSLLRCESV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564374726  540 GPAHSDGRFELVFSGKKLALRASSQDEAEDWLDRVREALQKVRP 583
Cdd:cd13321    89 GPAHSDGRFELVFPGKKLALRAPSRDEAEDWLDRIREALQKVRP 132
RUN_PLEKHM1 cd17679
RUN domain found in pleckstrin homology domain-containing family M member 1 (PLEKHM1) and ...
 1-139 6.40e-69

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: 227.47  E-value: 6.40e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKYIRAEAGGKRKKHThqkPLPQPVFWPLLKAVTHKHIISDLEHLVFINTDVGRCRAWLRLALNDG 80
Cdd:cd17679    36 LCCVLEAIFLHGLKDKFISKVSSVFSGDVD---KLPEPNFWPLLLKFSHRDVIDQIEHLSQITTDVGRCRAWIRLALNDG 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564374726   81 LMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKSAILNEW 139
Cdd:cd17679   113 LLESYLEAILKDKSALKSYYNPSAFLRDPEQLDILKSLLQGLESFQFELPYNSSLLNTW 171
RUN pfam02759
RUN domain; This domain is present in several proteins that are linked to the functions of ...
 1-133 1.40e-35

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: 131.63  E-value: 1.40e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726     1 MCSALEAVFIHGLHAKYIRAEAGGKRKkhthqkplPQPVFWPLLKAVT-----HKHIISDLEHLVFINT---DVGRCRAW 72
Cdd:pfam02759    2 LCAALEALLSHGLKRSSLLILRAAGLL--------PERSFWALLERVGklvppAEELLSSVQELEQIHTpysPDGRGRAW 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564374726    73 LRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYKS 133
Cdd:pfam02759   74 IRLALNEKLLDQWLKLLLSNKELLSEYYEPWALLADPEFGEILLGLLVGLSALDFNLCLKL 134
RUN cd17671
RUN domain; RUN domain, named after RPIP8 (Rap2 interacting protein 8), UNC-14 and NESCA (new ...
 2-129 1.58e-29

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: 114.83  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    2 CSALEAVFIHGLHAKYIRAEaggkrkkhthqkplpQPVFWPLLKAVTH-------KHIISDLEHLVFINTDVGRCRAWLR 74
Cdd:cd17671    35 CAALEAILSHGLKPKRFGGG---------------KVSFWDFLEALEKllpapslKQAIRDINSLSNVKTDDGRGRAWIR 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564374726   75 LALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17671   100 LALNEKSLESYLAALLSDQSLLRKYYEPWALLRDPEEAELFLSLLVGLSSLDFNL 154
RUN_SNX29 cd17689
RUN domain found in sorting nexin-29 (SNX29) and similar proteins; SNX29, also called RUN ...
 2-130 7.67e-26

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: 105.01  E-value: 7.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    2 CSALEAVFIHGLHAKY----IRAEAGGKRKKHTHQKPLPQ-PVFWPLLKAVTHKHIISDLEHLVFINTDVGRCRAWLRLA 76
Cdd:cd17689    31 CAQLEAVLQHGLKTSRspnlVSSAVTQVSGLAGSLGSAETePTFWPFVKEHLTKHELERFELLKNIWTDIGRGRAWLRSA 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564374726   77 LNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELS 130
Cdd:cd17689   111 LNEHSLERYLHILLSNENLLRQYYEDWAFLRDEERSSMLPNMAAGLGSILFALS 164
RUN_PLEKHM2 cd17680
RUN domain found in pleckstrin homology domain-containing family M member 2 (PLEKHM2) and ...
 2-129 4.97e-23

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: 96.16  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    2 CSALEAVFIHGLhakyiraeaggKRKKHThqkplpqpvFWPLLKAVTHKHIISDLEHLVFINTDVGRCRAWLRLALNDGL 81
Cdd:cd17680    38 CEALDHALLHGL-----------RRGNRG---------YWPFVKEFTHKETIKQIENLPNVTTDLGRGRAWLYLALNEGS 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564374726   82 MECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17680    98 LESYLRSFLENRKLVKKFYHKHALLRDSQRLELLLTLLSGLEFVQFDL 145
RUN smart00593
domain involved in Ras-like GTPase signaling;
69-132 1.17e-16

domain involved in Ras-like GTPase signaling;


Pssm-ID: 214736 [Multi-domain]  Cd Length: 64  Bit Score: 74.96  E-value: 1.17e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564374726     69 CRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFELSYK 132
Cdd:smart00593    1 FRAWIRLALNEKLLSSWLNLLLSDEELLSKYYEPWAFLRDPEEGEQLLGLLVGLSALDFNLPVD 64
RUN_RUFY1_like cd17681
RUN domain found in RUN and FYVE domain-containing proteins, RUFY1, RUFY2, RUFY3 and similar ...
 1-129 8.08e-13

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: 67.21  E-value: 8.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKyiraeaggKRKKHthqkplPQPVFWPLLKAVTH-----KHIISDLEHLVFINTDVGRCRAWLRL 75
Cdd:cd17681    37 FFVILEHVLRHGLKVK--------KSFLG------PNKSFWPVLEHVEKlvpeaNEITASVRDLPGIKTPLGRARAWLRL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564374726   76 ALNDGLMECYLKLLLQEPARLCEYYQPTALLRDaEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17681   103 ALMQKKLADYFRALIENKDLLSEFYEPGALMMS-EEAVVIAGLLVGLNVIDCNL 155
RUN1_DENND5B cd17691
RUN1 domain found in DENN domain-containing protein 5B (DENND5B) and similar proteins; DENND5B, ...
 1-127 2.54e-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: 61.22  E-value: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAK---------YIRAEAGGKRKKHTHQKPLP---------QPVFWPLLKAvthkHIISDLEH---L 59
Cdd:cd17691    55 LCDLLERIWSHGLQVKqgksalwshLLHFQEREEKQEHVAESPVAnglerrkseTGVNLPTLRV----SLIQDMRHiqnM 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564374726   60 VFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSF 127
Cdd:cd17691   131 SEIKTDVGRARAWIRLSLEKKLLSQHLKQLLSNQALTKKLYKRYAFLRCEEEKEQFLYHLLSLNAVDY 198
RUN1_DENND5 cd17677
RUN1 domain found in DENN domain-containing protein 5 (DENND5) and similar proteins; DENND5 ...
 1-125 3.42e-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: 60.10  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKyiraeaGGKRKKHTH----------QKPLPQPVFWPLlkavthKHIISDLEhlvfINTDVGRCR 70
Cdd:cd17677    55 LCDLLERIWSHGLQTK------QGKSALWSHllayqeneerLKPLPESLLFDM------KNVQNMKE----IKTDVGYAR 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564374726   71 AWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEfllSFLQGLTSL 125
Cdd:cd17677   119 AWIRLALEKKLLSKHLKTLLSNQDLLRSLYKRYAFLRCEDERE---QFLYHLLSL 170
RUN_RUFY4_like cd17682
RUN domain found in RUN and FYVE domain-containing protein 4 (RUFY4), FYVE and coiled-coil ...
 1-129 2.83e-09

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: 56.85  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAKYiraEAGGKRKKhthqkplpqpvFWPLLKAVTHKH--IISDLEHLV-FIN------TDVGRCRA 71
Cdd:cd17682    27 FCETLEKILRKGLKEKV---SLGGRRKD-----------YWDWLEELLKKLnkIPKSLSDAVkFVKsckkvkTNQGRGRL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564374726   72 WLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDAEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17682    93 FIRYALNKKCLHDPVQQLVKNPKLLSDYYSPDSILGNEILSEILLSLLYQLNEINFDL 150
RUN_RUNDC3 cd17684
RUN domain found in RUN domain-containing protein 3 (RUNDC3) and similar proteins; RUNDC3 ...
 2-129 3.06e-08

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: 53.94  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    2 CSALEAVFIHGLhaKYIRAEAGGKRKKHthqkplpqpvFWPLLKaVTHKHI----ISDLEHLVFINTDVGRCRAWLRLAL 77
Cdd:cd17684    33 AAILEQILSHRL--KPVKPWYGSEEPRT----------FWDYIR-VACKKVpqncIASIEQMENIKSPKAKGRAWIRVAL 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564374726   78 NDGLMECYLKLLLQEPARLCEYYQPTALLRdAEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17684   100 MEKRLSEYLSTALKQTRLTRNFYQDGAIML-SEDATVLCGMLIGLNAIDFSF 150
RUN1_DENND5A cd17690
RUN1 domain found in DENN domain-containing protein 5A (DENND5A) and similar proteins; DENND5A, ...
 1-118 1.72e-06

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: 50.01  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLHAK--------YIRAEAGGKRKKHT--------------HQKPLPQPVFWPLLKAVTH--KHIisdl 56
Cdd:cd17690    55 LCDLLERIWSHGLQVKqgksalwsHLLHYQENRERKTTssglstsgiildseRRKSDASLAMPPLKISLIQdmRHI---- 130

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564374726   57 EHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLR-DAEEAEF---LLSF 118
Cdd:cd17690   131 QNIGEIKTDVGKARAWVRLSMEKKLLSRHLKQLLSDHELTKKLYKRYAFLRcDDEKEQFlyhLLSF 196
RUN_RUFY2 cd17695
RUN domain found in RUN and FYVE domain-containing protein 2 (RUFY2) and similar proteins; ...
 52-129 2.95e-06

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: 48.05  E-value: 2.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564374726   52 IISDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDaEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17695    79 IAASVRDLPGLKTPLGRARAWLRLALMQKKLADYLRCLIIRRDLLSEFYEYHALMME-EEGAVIVGLLVGLNVIDANL 155
RUN_RUFY3 cd17696
RUN domain found in RUN and FYVE domain-containing protein 3 (RUFY3) and similar proteins; ...
 40-129 3.36e-06

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: 48.07  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   40 FWPLLKAVTH-----KHIISDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDaEEAEF 114
Cdd:cd17696    62 FWGPLELVEKlvpeaAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINRKDLLSEFYEPNALMME-EEGAI 140

                          90
                  ....*....|....*
gi 564374726  115 LLSFLQGLTSLSFEL 129
Cdd:cd17696   141 IAGLLVGLNVIDANF 155
RUN_RUFY1 cd17694
RUN domain found in RUN and FYVE domain-containing protein 1 (RUFY1) and similar proteins; ...
 52-129 3.65e-06

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: 47.98  E-value: 3.65e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564374726   52 IISDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRDaEEAEFLLSFLQGLTSLSFEL 129
Cdd:cd17694    79 IATSARNLPELKTAVGRGRAWLHLALMQKKLADYLKVLIDRKDLLSEFYEPGALMME-EEGAVIVGLLVGLNVIDANL 155
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 493-574 6.33e-06

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: 45.61  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  493 GTVARRGA--MGIWKEFFCELSPLELRLYLSDEERT--CVESCSLLRCEAVGPAHSDGR---FELVFS-GKKLALRASSQ 564
Cdd:cd00821     3 GYLLKRGGggLKSWKKRWFVLFEGVLLYYKSKKDSSykPKGSIPLSGILEVEEVSPKERphcFELVTPdGRTYYLQADSE 82

                          90
                  ....*....|
gi 564374726  565 DEAEDWLDRV 574
Cdd:cd00821    83 EERQEWLKAL 92
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 489-579 6.95e-06

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: 45.62  E-value: 6.95e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    489 LMKLGTVARRGamgiWKEFFCELSPLELRLYLSDEER---TCVESCSLLRCEAVGPAHSDGR-----FELVFS-GKKLAL 559
Cdd:smart00233    7 LYKKSGGGKKS----WKKRYFVLFNSTLLYYKSKKDKksyKPKGSIDLSGCTVREAPDPDSSkkphcFEIKTSdRKTLLL 82

                            90       100
                    ....*....|....*....|
gi 564374726    560 RASSQDEAEDWLDRVREALQ 579
Cdd:smart00233   83 QAESEEEREKWVEALRKAIA 102
RUN_RUNDC3A cd17699
RUN domain found in RUN domain-containing protein 3A (RUNDC3A) and similar proteins; RUN ...
 37-127 3.59e-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: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   37 QPVFWPLLKAVTHK---HIISDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTA-LLRdaEEA 112
Cdd:cd17699    56 QRGFWDYIRLACSKvpnNCISSIENMENISTSRAKGRAWIRVALMEKRLSEYIATALRDTRTTRRFYDDGAiMLR--EES 133

                          90
                  ....*....|....*
gi 564374726  113 EFLLSFLQGLTSLSF 127
Cdd:cd17699   134 TVLTGMLIGLSAIDF 148
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 942-995 5.41e-05

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: 41.68  E-value: 5.41e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 564374726    942 HVYHCDLCTQRGFiCQICHHQDIIFpfeFDTTVRCAECRTVFHQSCQAVVRKGC 995
Cdd:smart00109    1 HKHVFRTFTKPTF-CCVCRKSIWGS---FKQGLRCSECKVKCHKKCADKVPKAC 50
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 640-732 7.95e-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: 39.84  E-value: 7.95e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    640 IKESLLYLYAD---RTWIPYIFSLSLESLKCFRVRNNEK--------MLSDShgveTIRDILPDTSLGGPAFFKIITA-K 707
Cdd:smart00233    2 IKEGWLYKKSGggkKSWKKRYFVLFNSTLLYYKSKKDKKsykpkgsiDLSGC----TVREAPDPDSSKKPHCFEIKTSdR 77

                            90       100
                    ....*....|....*....|....*
gi 564374726    708 AVLKLQAKNTEEAAHWRDLVRKVLA 732
Cdd:smart00233   78 KTLLLQAESEEEREKWVEALRKAIA 102
RUN_RUNDC3B cd17700
RUN domain found in RUN domain-containing protein 3B (RUNDC3B) and similar proteins; RUN ...
 40-127 1.43e-03

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: 40.34  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   40 FWPLLKAVTHK---HIISDLEHLVFINTDVGRCRAWLRLALNDGLMECYLKLLLQEPARLCEYYQPTALLRdAEEAEFLL 116
Cdd:cd17700    59 FWDYIRVACSKvphNCICSIENMENVSSSRAKGRAWIRVALMEKRLSEYISTALRDFKTTRRFYEDGAIVL-GEEANMLA 137

                          90
                  ....*....|.
gi 564374726  117 SFLQGLTSLSF 127
Cdd:cd17700   138 GMLLGLNAIDF 148
RUN_RUBCN cd17686
RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing ...
 1-116 1.75e-03

RUN domain found in Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (RUBCN) and similar proteins; RUBCN, also called rubicon, or beclin-1 associated RUN domain containing protein (Baron), is part of a Beclin-1-Vps34-containing autophagy complex. It negatively regulates endosome maturation and degradative endocytic trafficking and impairs autophagosome maturation process. It is also an important negative regulator of the innate immune response, enhances viral replication and may play a role in viral immune evasion. This model contains the RUN domain of RUBCN.


Pssm-ID: 439048  Cd Length: 151  Bit Score: 39.94  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726    1 MCSALEAVFIHGLhakyiRAEAGGKRkkhthqkplpQPVFWPLLKAVT--------HKHIISDLEHLVFINTDVGRcrAW 72
Cdd:cd17686    24 LCRAVENILQHGL-----KEFQGLNK----------EIDDWEFVQGLRwlqptlapSIEQQSRSSPSESEVSDKGR--LW 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564374726   73 LRLALNDG-LMECyLKLLLQEPARLCEYYQPTALLRDAEEAEFLL 116
Cdd:cd17686    87 LRQSLQQHcLSSQ-LQWLVSDKELLRKYYEDEAFLRQEGYATALL 130
PH_GAP1-like cd01244
RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; ...
 658-733 3.54e-03

RAS p21 protein activator (GTPase activating protein) family pleckstrin homology (PH) domain; RASAL1, GAP1(m), GAP1(IP4BP), and CAPRI are all members of the GAP1 family of GTPase-activating proteins. They contain N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. With the notable exception of GAP1(m), they all possess an arginine finger-dependent GAP activity on the Ras-related protein Rap1. They act as a suppressor of RAS enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. PH domains share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 269950  Cd Length: 107  Bit Score: 38.04  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  658 FSLSLESLKCFRVRNNEKM----LSDSHGVETIRDilpdTSLGGPAFFKIITAKAVLKLQAKNTEEAAHWRDLVRKVLAS 733
Cdd:cd01244    26 FRLTNEALSYSKSKGKQPLcsipLEDILAVERVEE----ESFKMKNMFQIVQPDRTLYLQAKNVVELNEWLSALRKVCLC 101
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 489-578 5.27e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726   489 LMKLGTVARRGamgiWKEFFCELSPLELRLYLSDEERTC--------VESCSLLRCEAVGPAHSDGRFELVFS----GKK 556
Cdd:pfam00169    7 LLKKGGGKKKS----WKKRYFVLFDGSLLYYKDDKSGKSkepkgsisLSGCEVVEVVASDSPKRKFCFELRTGertgKRT 82

                           90       100
                   ....*....|....*....|..
gi 564374726   557 LALRASSQDEAEDWLDRVREAL 578
Cdd:pfam00169   83 YLLQAESEEERKDWIKAIQSAI 104
PH_DAPP1 cd10573
Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; ...
 482-575 5.65e-03

Dual Adaptor for Phosphotyrosine and 3-Phosphoinositides Pleckstrin homology (PH) domain; DAPP1 (also known as PHISH/3' phosphoinositide-interacting SH2 domain-containing protein or Bam32) plays a role in B-cell activation and has potential roles in T-cell and mast cell function. DAPP1 promotes B cell receptor (BCR) induced activation of Rho GTPases Rac1 and Cdc42, which feed into mitogen-activated protein kinases (MAPK) activation pathways and affect cytoskeletal rearrangement. DAPP1can also regulate BCR-induced activation of extracellular signal-regulated kinase (ERK), and c-jun NH2-terminal kinase (JNK). DAPP1 contains an N-terminal SH2 domain and a C-terminal pleckstrin homology (PH) domain with a single tyrosine phosphorylation site located centrally. DAPP1 binds strongly to both PtdIns(3,4,5)P3 and PtdIns(3,4)P2. The PH domain is essential for plasma membrane recruitment of PI3K upon cell activation. 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: 269977 [Multi-domain]  Cd Length: 96  Bit Score: 37.30  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564374726  482 LSNPFRGLMKLGTVARRgamgiWKEFFCELSPLELRLYLSDEERTCVESCSLLRCEAVGPAHSDGR---FELVFSGKKLA 558
Cdd:cd10573     2 LGSKEGYLTKLGGIVKN-----WKTRWFVLRRNELKYFKTRGDTKPIRVLDLRECSSVQRDYSQGKvncFCLVFPERTFY 76

                          90
                  ....*....|....*..
gi 564374726  559 LRASSQDEAEDWLDRVR 575
Cdd:cd10573    77 MYANTEEEADEWVKLLK 93
 
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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