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Conserved domains on  [gi|1190405189|ref|XP_020852755|]
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rho GTPase-activating protein 22 isoform X7 [Phascolarctos cinereus]

Protein Classification

PH-like and RhoGAP_ARHGAP22_24_25 domain-containing protein( domain architecture ID 10351259)

protein containing domains PH-like, RhoGAP_ARHGAP22_24_25, and SMC_N

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
77-275 8.37e-138

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 400.67  E-value: 8.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  77 GIFGQRLEDTVQYERKYGHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390     1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLAT 236
Cdd:cd04390    81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1190405189 237 VFGPNILRPKKEDPVTIMEGTSLVQHLMTILISKHSQLF 275
Cdd:cd04390   161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
12-61 3.19e-27

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13378:

Pssm-ID: 473070  Cd Length: 116  Bit Score: 106.57  E-value: 3.19e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190405189  12 HLRE-SKGGSGDREKMPVNHEAFLLMANSQNDMEDWVKAIRRVIWAPFGGG 61
Cdd:cd13378    66 HLFEiLPGGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
HFD_SF super family cl45933
histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally ...
535-617 1.07e-05

histone fold domain (HFD) superfamily; The histone fold domain (HFD) is a structurally conserved interaction motif involved in heterodimerization of the core histones and their assembly into the nucleosome octamer. Histone fold heterodimers play crucial roles in gene regulation. The minimal HFD consists of three alpha helices connected by two short, unstructured loops. The HFD is found in core histones, TATA box-binding protein-associated factors (TAFs), and many other transcription factors. HFD plays a role in the nucleosomal core particle by conserving histone interactions; these contain more than one HFD. The structure of the nucleosome core particle has two modes that have the largest interaction surfaces, and these are the H3-H4 and H2A-H2B heterodimer interactions. Several TAFs interact via histone-fold (HF) motifs. Five HF-containing TAF pairs have been described in transcription factor II D (TFIID): TAF6-TAF9, TAF4-TAF12, TAF11-TAF13, TAF8-TAF10 and TAF3-TAF10.


The actual alignment was detected with superfamily member cd08045:

Pssm-ID: 480273 [Multi-domain]  Cd Length: 100  Bit Score: 44.53  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 535 NNFNSMSRDSAQC-SHALQ----SLVTELkAELSKQRTEYETSLRRIeEASSSLKKQMARLEEdLDQERKKftmleiRLR 609
Cdd:cd08045    21 HGLKEVSPDVLSLlSLAVQerlrDLLEKL-IVASKHRVDSEKPDYRY-EVTSDVRRQLKALER-LEREEEE------RRR 91

                  ....*...
gi 1190405189 610 NSERARED 617
Cdd:cd08045    92 EEERERLL 99
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
77-275 8.37e-138

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 400.67  E-value: 8.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  77 GIFGQRLEDTVQYERKYGHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390     1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLAT 236
Cdd:cd04390    81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1190405189 237 VFGPNILRPKKEDPVTIMEGTSLVQHLMTILISKHSQLF 275
Cdd:cd04390   161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
99-246 1.19e-58

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 193.92  E-value: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDF 177
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190405189 178 LSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPK 246
Cdd:pfam00620  81 IEAAKL--PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
99-271 1.46e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 194.41  E-value: 1.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189   99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDF 177
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPdLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  178 LSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIMEgT 257
Cdd:smart00324  84 IEAAKL--EDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160
                          170
                   ....*....|....
gi 1190405189  258 SLVQHLMTILISKH 271
Cdd:smart00324 161 RHQNTVIEFLIENA 174
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
12-61 3.19e-27

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241529  Cd Length: 116  Bit Score: 106.57  E-value: 3.19e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190405189  12 HLRE-SKGGSGDREKMPVNHEAFLLMANSQNDMEDWVKAIRRVIWAPFGGG 61
Cdd:cd13378    66 HLFEiLPGGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
HFD_TAF4 cd08045
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
535-617 1.07e-05

histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.


Pssm-ID: 467027 [Multi-domain]  Cd Length: 100  Bit Score: 44.53  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 535 NNFNSMSRDSAQC-SHALQ----SLVTELkAELSKQRTEYETSLRRIeEASSSLKKQMARLEEdLDQERKKftmleiRLR 609
Cdd:cd08045    21 HGLKEVSPDVLSLlSLAVQerlrDLLEKL-IVASKHRVDSEKPDYRY-EVTSDVRRQLKALER-LEREEEE------RRR 91

                  ....*...
gi 1190405189 610 NSERARED 617
Cdd:cd08045    92 EEERERLL 99
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
551-638 1.50e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  551 LQSLVTELKAELSKQRTEYETSLRRIEEASS----SLKK------QMARLEEDLDQERKkftmleirlrnserAREDAEK 620
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALARLEEETAqknnALKKireleaQISELQEDLESERA--------------ARNKAEK 292
                           90       100
                   ....*....|....*....|..
gi 1190405189  621 RNQLLQKEME----EFFSTLGT 638
Cdd:pfam01576  293 QRRDLGEELEalktELEDTLDT 314
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
549-632 6.23e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 549 HALQSLVTELkAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERARE---------DAE 619
Cdd:COG1579    24 HRLKELPAEL-AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqkeieSLK 102
                          90
                  ....*....|...
gi 1190405189 620 KRNQLLQKEMEEF 632
Cdd:COG1579   103 RRISDLEDEILEL 115
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
548-631 6.04e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  548 SHALQSLVTELKAELSKQRTEYETSLRRIEEASSSLKKQMARL-EEDLDQERKKFTMLEIRLRNSER-AREDAEKRNQLL 625
Cdd:smart00935  13 SPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQkLQQDLQKRQQEE 92

                   ....*.
gi 1190405189  626 QKEMEE 631
Cdd:smart00935  93 LQKILD 98
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-636 1.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 551 LQSLVTELK--AELSKQRTEYETSLRRIEEASSSLKKQMARL----EEDLD---QERKKFTMLEIRLRNSERAREDAEKR 621
Cdd:PRK03918  541 IKSLKKELEklEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEerlKELEPFYNEYLELKDAEKELEREEKE 620
                          90
                  ....*....|....*
gi 1190405189 622 NQLLQKEMEEFFSTL 636
Cdd:PRK03918  621 LKKLEEELDKAFEEL 635
PH pfam00169
PH domain; PH stands for pleckstrin homology.
29-54 6.89e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 36.77  E-value: 6.89e-03
                          10        20
                  ....*....|....*....|....*.
gi 1190405189  29 NHEAFLLMANSQNDMEDWVKAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
539-632 7.15e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  539 SMSRDSAQCSHALQSLVTELKaELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERK-------KFTMLEIRLRNS 611
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLARL 738
                           90       100
                   ....*....|....*....|.
gi 1190405189  612 ERAREDAEKRNQLLQKEMEEF 632
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTEL 759
 
Name Accession Description Interval E-value
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
77-275 8.37e-138

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 400.67  E-value: 8.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  77 GIFGQRLEDTVQYERKYGHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASL 156
Cdd:cd04390     1 GVFGQRLEDTVAYERKFGPRLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLAT 236
Cdd:cd04390    81 LKLYLRELPEPVIPWAQYEDFLSCAQLLSKDEEKGLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLAT 160
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1190405189 237 VFGPNILRPKKEDPVTIMEGTSLVQHLMTILISKHSQLF 275
Cdd:cd04390   161 VFGPNILRPKVEDPATIMEGTPQIQQLMTVMISKHEPLF 199
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
99-267 2.04e-63

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 207.15  E-value: 2.04e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 SCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIMEGTS 258
Cdd:cd00159    81 ELAKI--EDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDDELLEDIKK 158

                  ....*....
gi 1190405189 259 LVQHLMTIL 267
Cdd:cd00159   159 LNEIVEFLI 167
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
99-246 1.19e-58

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 193.92  E-value: 1.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDF 177
Cdd:pfam00620   1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVdLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190405189 178 LSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPK 246
Cdd:pfam00620  81 IEAAKL--PDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPP 147
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
99-271 1.46e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 194.41  E-value: 1.46e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189   99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKP-LFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDF 177
Cdd:smart00324   4 PIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPdLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEEF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  178 LSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIMEgT 257
Cdd:smart00324  84 IEAAKL--EDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVASLKD-I 160
                          170
                   ....*....|....
gi 1190405189  258 SLVQHLMTILISKH 271
Cdd:smart00324 161 RHQNTVIEFLIENA 174
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
78-268 8.21e-43

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 152.62  E-value: 8.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  78 IFG---QRLEDTVQYERKyghrlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVA 154
Cdd:cd04393     2 VFGvplQELQQAGQPENG-----VPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 155 SLLKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTlELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNL 234
Cdd:cd04393    77 SLLRLFLQELPEGLIPASLQIRLMQLYQDYNGEDEFGR-KLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENL 155
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1190405189 235 ATVFGPNI--LRPKKEDpvtiMEGTSLVQHLMTILI 268
Cdd:cd04393   156 AAVFGPDVfhVYTDVED----MKEQEICSRIMAKLL 187
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
74-247 9.84e-42

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 149.80  E-value: 9.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  74 LPQGIFGQRLEDTVqyERKYGHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTV 153
Cdd:cd04404     1 LPTQQFGVSLQFLK--EKNPEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNMGEPVDFDQYEDVHLP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 154 ASLLKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELakqVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQN 233
Cdd:cd04404    79 AVILKTFLRELPEPLLTFDLYDDIVGFLNVDKEERVERVKQL---LQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSN 155
                         170
                  ....*....|....
gi 1190405189 234 LATVFGPNILRPKK 247
Cdd:cd04404   156 LAVVFGPNLLWAKD 169
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
75-275 6.93e-41

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 147.99  E-value: 6.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  75 PQGIFGQRLEDTVqyeRKYGHRLApLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCG--EKPLFDSTTDVHT 152
Cdd:cd04386     1 EKPVFGTPLEEHL---KRTGREIA-LPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGtfSLPLDEFYSDPHA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 153 VASLLKLYLRELPEPVIPFAKYEDFLSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQ 232
Cdd:cd04386    77 VASALKSYLRELPDPLLTYNLYEDWVQAANK--PDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1190405189 233 NLATVFGPNILRPKKEDPVTIMEGTSLVQHLMTI--LISKHSQLF 275
Cdd:cd04386   155 NIAIVLAPNLLWAKNEGSLAEMAAGTSVHVVAIVelIISHADWFF 199
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
79-275 5.26e-38

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 139.46  E-value: 5.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYErkygHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCG-------EKPLFDSttDVH 151
Cdd:cd04398     1 FGVPLEDLILRE----GDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDplnvlliSPEDYES--DIH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 152 TVASLLKLYLRELPEPVIPFAKYEDFLSCAQllSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSV 231
Cdd:cd04398    75 SVASLLKLFFRELPEPLLTKALSREFIEAAK--IEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1190405189 232 QNLATVFGPNILrpkKEDPVTIMEGTSLVQhLMTILISKHSQLF 275
Cdd:cd04398   153 NNLAIIWGPTLM---NAAPDNAADMSFQSR-VIETLLDNAYQIF 192
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
78-242 1.68e-35

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 132.48  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  78 IFGQRLEDTVQYE-RKYGHRLAPLLVEQCVDFI-RERGLTEEGLFRMPGQANLVKDLQDSFDC-GEKPLFDSTT--DVHT 152
Cdd:cd04400     1 IFGSPLEEAVELSsHKYNGRDLPSVVYRCIEYLdKNRAIYEEGIFRLSGSASVIKQLKERFNTeYDVDLFSSSLypDVHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 153 VASLLKLYLRELPEPVIPFAKYEDFLSCAQLLSkDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQ 232
Cdd:cd04400    81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENH-DRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLR 159
                         170
                  ....*....|..
gi 1190405189 233 NLATVFGP--NI 242
Cdd:cd04400   160 NVCIVFSPtlNI 171
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
79-275 2.88e-35

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 131.75  E-value: 2.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDT-VQYERKYghrlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCG--EKPLFDST-TDVHTVA 154
Cdd:cd04395     2 FGVPLDDCpPSSENPY----VPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGgfDIDLQDPRwRDVNVVS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 155 SLLKLYLRELPEPVIPFAKYEDFLSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNL 234
Cdd:cd04395    78 SLLKSFFRKLPEPLFTNELYPDFIEANRI--EDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNL 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1190405189 235 ATVFGPNILRPKKEDPVTIMEGTSLVQHLMTILISKHSQLF 275
Cdd:cd04395   156 AIVFGPTLVRTSDDNMETMVTHMPDQCKIVETLIQHYDWFF 196
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
99-269 5.36e-35

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 130.88  E-value: 5.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04382    18 PALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKEFM 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 SCAQLLSKDESEgtLELAKQVKNLPQANYNLLKYICKFLDEVqAHSNINKMSVQNLATVFGPNIL--RPKKEDPVTIMEG 256
Cdd:cd04382    98 EAAEILDEDNSR--AALYQAISELPQPNRDTLAFLILHLQRV-AQSPECKMDINNLARVFGPTIVgySVPNPDPMTILQD 174
                         170
                  ....*....|...
gi 1190405189 257 TSLVQHLMTILIS 269
Cdd:cd04382   175 TVRQPRVVERLLE 187
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-275 2.20e-34

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 129.56  E-value: 2.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDC-GEKPLFDSTT--DVHTVASLLKLYLRELPEPVIPFAKYE 175
Cdd:cd04372    17 PMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRdGEKADISATVypDINVITGALKLYFRDLPIPVITYDTYP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 176 DFLSCAQLLSKDESegtLELAKQ-VKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIM 254
Cdd:cd04372    97 KFIDAAKISNPDER---LEAVHEaLMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPEDSALTTL 173
                         170       180
                  ....*....|....*....|.
gi 1190405189 255 EGTSLVQHLMTILISKHSQLF 275
Cdd:cd04372   174 NDMRYQILIVQLLITNEDVLF 194
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
79-248 1.09e-32

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 124.43  E-value: 1.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYErkygHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTT--DVHTVASL 156
Cdd:cd04403     1 FGCHLEALCQRE----NSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLDLDDSKweDIHVITGA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQL-LSKDESEGTLELakqVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLA 235
Cdd:cd04403    77 LKLFFRELPEPLFPYSLFNDFVAAIKLsDYEQRVSAVKDL---IKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLA 153
                         170
                  ....*....|...
gi 1190405189 236 TVFGPNILRPKKE 248
Cdd:cd04403   154 IVFGPTLLRPEQE 166
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
77-251 2.73e-32

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 123.30  E-value: 2.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  77 GIFGQRLEDTVQYERKyghrLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTT--DVHTVA 154
Cdd:cd04383     1 KLFNGSLEEYIQDSGQ----AIPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFERGEDPLADDQNdhDINSVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 155 SLLKLYLRELPEPVIPFAKYEDFLSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNL 234
Cdd:cd04383    77 GVLKLYFRGLENPLFPKERFEDLMSCVKL--ENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNL 154
                         170
                  ....*....|....*...
gi 1190405189 235 ATVFGPNILR-PKKEDPV 251
Cdd:cd04383   155 AICFGPTLMPvPEGQDQV 172
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-275 1.07e-30

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 119.47  E-value: 1.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04376    10 PRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTAFI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 ScAQLLSKDESEGTLELAKQVknLPQANYNLLKYICKFLDEVQAHSNI-----------NKMSVQNLATVFGPNILRPKK 247
Cdd:cd04376    90 G-TALLEPDEQLEALQLLIYL--LPPCNCDTLHRLLKFLHTVAEHAADsidedgqevsgNKMTSLNLATIFGPNLLHKQK 166
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1190405189 248 -------EDPVTIMEGTSLVQHLMTiLISKHSQLF 275
Cdd:cd04376   167 sgerefvQASLRIEESTAIINVVQT-MIDNYEELF 200
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
79-268 1.86e-30

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 117.88  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYER-KYGHRLAPLLVEQCVDFIRERGLTE-EGLFRMPGQANLVKDLQDSFDCGEKPLfDSTTDVHTVASL 156
Cdd:cd04389     1 FGSSLEEIMDRQKeKYPELKLPWILTFLSEKVLALGGFQtEGIFRVPGDIDEVNELKLRVDQWDYPL-SGLEDPHVPASL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLScaqllSKDESEGTLELakqVKNLPQANYNLLKYICKFLDEVQAHSNI--NKMSVQNL 234
Cdd:cd04389    80 LKLWLRELEEPLIPDALYQQCIS-----ASEDPDKAVEI---VQKLPIINRLVLCYLINFLQVFAQPENVahTKMDVSNL 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1190405189 235 ATVFGPNILRPKKEDPVTIMEGTSLVQHLMTILI 268
Cdd:cd04389   152 AMVFAPNILRCTSDDPRVIFENTRKEMSFLRTLI 185
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
79-258 1.18e-29

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 115.61  E-value: 1.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYERKyghrlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLK 158
Cdd:cd04377     1 FGVSLSSLTSEDRS-----VPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 159 LYLRELPEPVIPFAKYEDFLSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVF 238
Cdd:cd04377    76 QWLRELPEPLMTFELYENFLRAMEL--EEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVF 153
                         170       180
                  ....*....|....*....|.
gi 1190405189 239 GPNILR-PKKEDPVTIMEGTS 258
Cdd:cd04377   154 APCILRcPDTADPLQSLQDVS 174
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
102-255 3.82e-29

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 114.80  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 102 VEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSF------DCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYE 175
Cdd:cd04374    32 VRKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpktsTPGDVDLDNSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 176 DFLSCAQLLSKDESEGtlELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIME 255
Cdd:cd04374   112 DFINAAKSENLESRVN--AIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEETVAAIMD 189
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
99-260 3.67e-28

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 112.13  E-value: 3.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGeKPLFD-STTDVHTVASLLKLYLRELPEPVIPFAKYEDF 177
Cdd:cd04378    17 PFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENG-KDLVElSELSPHDISSVLKLFLRQLPEPLILFRLYNDF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 178 LSCAQLLSKDESEGT--------LELAKQVKNL----PQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRP 245
Cdd:cd04378    96 IALAKEIQRDTEEDKapntpievNRIIRKLKDLlrqlPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIRP 175
                         170
                  ....*....|....*.
gi 1190405189 246 KKED-PVTImegTSLV 260
Cdd:cd04378   176 RPGDaDVSL---SSLV 188
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
99-268 1.31e-27

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 110.08  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04407    16 PIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRELPEPLMTFAQYNDFL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 SCAQLLSKDESegTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILR-PKKEDPVTIMEGT 257
Cdd:cd04407    96 RAVELPEKQEQ--LQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRcPDSSDPLTSMKDV 173
                         170
                  ....*....|.
gi 1190405189 258 SLVQHLMTILI 268
Cdd:cd04407   174 AKTTTCVEMLI 184
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
99-265 1.94e-27

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 109.32  E-value: 1.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSF--DCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYED 176
Cdd:cd04385    16 PVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFrkDARSVQLREGEYTVHDVADVLKRFLRDLPDPLLTSELHAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 177 FLSCAQLlsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTIMEG 256
Cdd:cd04385    96 WIEAAEL--ENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQTDEHSVGQTSHE 173

                  ....*....
gi 1190405189 257 TSLVQHLMT 265
Cdd:cd04385   174 VKVIEDLID 182
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
79-268 2.50e-27

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 109.08  E-value: 2.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYERKYghrlaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDC-GEKPLFDSTTDVHTVASLL 157
Cdd:cd04373     1 FGVPLANVVTSEKPI-----PIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQdHNLDLVSKDFTVNAVAGAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 158 KLYLRELPEPVIPFAKYEDFLSCAQLLskDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATV 237
Cdd:cd04373    76 KSFFSELPDPLIPYSMHLELVEAAKIN--DREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSIC 153
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1190405189 238 FGPNILRPKKEDpVTIMEGTSLVQHLMTILI 268
Cdd:cd04373   154 FWPTLMRPDFTS-MEALSATRIYQTIIETFI 183
PH_RhoGAP2 cd13378
Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 ...
12-61 3.19e-27

Rho GTPase activating protein 2 Pleckstrin homology (PH) domain; RhoGAP2 (also called RhoGap22 or ArhGap22) are involved in cell polarity, cell morphology and cytoskeletal organization. They activate a GTPase belonging to the RAS superfamily of small GTP-binding proteins. The encoded protein is insulin-responsive, is dependent on the kinase Akt, and requires the Akt-dependent 14-3-3 binding protein which binds sequentially to two serine residues resulting in regulation of cell motility. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241529  Cd Length: 116  Bit Score: 106.57  E-value: 3.19e-27
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1190405189  12 HLRE-SKGGSGDREKMPVNHEAFLLMANSQNDMEDWVKAIRRVIWAPFGGG 61
Cdd:cd13378    66 HLFEiLPGGAGDREKVPMNHEAFLLMANSQSDMEDWVKAIRRVIWAPFGGG 116
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
97-249 9.26e-27

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 107.71  E-value: 9.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  97 LAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFD--STTDVHTVASLLKLYLRELPEPVIP---F 171
Cdd:cd04387    15 KVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKDVSVmlSEMDVNAIAGTLKLYFRELPEPLFTdelY 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1190405189 172 AKYEDFLSCAQLLSKDESEGTLelakqVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKED 249
Cdd:cd04387    95 PNFAEGIALSDPVAKESCMLNL-----LLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTLLRPSEKE 167
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
78-243 1.81e-26

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 107.88  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  78 IFGQRLEDTVQYER-------------KYGHrlAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGE---K 141
Cdd:cd04396     1 VFGVSLEESLKYASvaisivdedgeqyVYGY--IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 142 PLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDF---------------LSCAQLLSKDESEGTLELAKQVKNLPQAN 206
Cdd:cd04396    79 SFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLYEEFrnplrkrprilqymkGRINEPLNTDIDQAIKEYRDLITRLPNLN 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1190405189 207 YNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNIL 243
Cdd:cd04396   159 RQLLLYLLDLLAVFARNSDKNLMTASNLAAIFQPGIL 195
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-247 9.15e-26

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 104.89  E-value: 9.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEeGLFRMPGQANLVKDLQDSFDCGEKP---LFDSTTDVHTVASLLKLYLRELPEPVIPFAKYE 175
Cdd:cd04384    19 PQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIPdltKDVYIQDIHSVSSLCKLYFRELPNPLLTYQLYE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190405189 176 DFlscAQLLSKDESEGTLELAKQV-KNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKK 247
Cdd:cd04384    98 KF---SEAVSAASDEERLEKIHDViQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSKQ 167
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-262 1.56e-25

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 104.89  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04409    17 PFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEFI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 SCAQ------------LLSKDESEGT--------LELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVF 238
Cdd:cd04409    97 GLAKesqhvnetqeakKNSDKKWPNMctelnrilLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGIIF 176
                         170       180
                  ....*....|....*....|....*
gi 1190405189 239 GPNILRPKKED-PVTImegTSLVQH 262
Cdd:cd04409   177 GPTLIRPRPTDaTVSL---SSLVDY 198
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-275 5.30e-25

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 102.76  E-value: 5.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTdVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04402    16 PKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVEVDLKAEP-VLLLASVLKDFLRNIPGSLLSSDLYEEWM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 179 SCAQllSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTiMEGTS 258
Cdd:cd04402    95 SALD--QENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWPPASSELQ-NEDLK 171
                         170
                  ....*....|....*..
gi 1190405189 259 LVQHLMTILISKHSQLF 275
Cdd:cd04402   172 KVTSLVQFLIENCQEIF 188
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
79-276 1.73e-24

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 101.77  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYERkyGHRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPL---FDSTTDVHTVAS 155
Cdd:cd04379     1 FGVPLSRLVEREG--ESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVelsEELYPDINVITG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 156 LLKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAKQVKN-LPQANYNLLKYICKFLDEVQAHSNINKMSVQNL 234
Cdd:cd04379    79 VLKDYLRELPEPLITPQLYEMVLEALAVALPNDVQTNTHLTLSIIDcLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1190405189 235 ATVFGPNILRPKKEDPVTIMEGTSLVQHLMTILISKHSQLFS 276
Cdd:cd04379   159 AVCFGPVLMFCSQEFSRYGISPTSKMAAVSTVDFKQHIEVLH 200
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
79-242 1.78e-24

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 100.97  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQYERKY-GHRLaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTtDVHTVASLL 157
Cdd:cd04381     1 FGASLSLAVERSRCHdGIDL-PLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRRESPNLEEY-EPPTVASLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 158 KLYLRELPEPVIP---FAKYEDflSCAQllsKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNL 234
Cdd:cd04381    79 KQYLRELPEPLLTkelMPRFEE--ACGR---PTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNI 153

                  ....*...
gi 1190405189 235 ATVFGPNI 242
Cdd:cd04381   154 SIVLSPTV 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
99-275 2.21e-24

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 101.65  E-value: 2.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQA----NLVKDLQDSFDCGEKpLFDSTTdVHTVASLLKLYLRELPEPVIPFAKY 174
Cdd:cd04391    23 PLIFQKLINKLEERGLETEGILRIPGSAqrvkFLCQELEAKFYEGTF-LWDQVK-QHDAASLLKLFIRELPQPLLTVEYL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 175 EDFLSCAQLLSKDESEGTLELAkqVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDPVTI- 253
Cdd:cd04391   101 PAFYSVQGLPSKKDQLQALNLL--VLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMIMAPNLFPPRGKHSKDNe 178
                         170       180
                  ....*....|....*....|....*..
gi 1190405189 254 -----MEGTSLVQHLMTILISKHSQLF 275
Cdd:cd04391   179 slqeeVNMAAGCANIMRLLIRYQDLLW 205
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
78-243 3.36e-24

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 100.62  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  78 IFGQRLED-TVQYERKYGHrLAPLLVEQCvDFIrERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLfdSTTDVHTVASL 156
Cdd:cd04394     1 VFGVPLHSlPHSTVPEYGN-VPKFLVDAC-TFL-LDHLSTEGLFRKSGSVVRQKELKAKLEGGEACL--SSALPCDVAGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAKQVknLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLAT 236
Cdd:cd04394    76 LKQFFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCL--LPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAV 153

                  ....*..
gi 1190405189 237 VFGPNIL 243
Cdd:cd04394   154 IFAPNLF 160
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
99-245 4.54e-23

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 97.19  E-value: 4.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  99 PLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFL 178
Cdd:cd04408    17 PFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLKELPEPVLPFQLYDDFI 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1190405189 179 SCAQLLSKD------ESEGTLELAKQVKNL----PQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRP 245
Cdd:cd04408    97 ALAKELQRDsekaaeSPSIVENIIRSLKELlgrlPVSNYNTLRHLMAHLYRVAERFEDNKMSPNNLGIVFGPTLLRP 173
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
102-277 8.05e-23

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 96.76  E-value: 8.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 102 VEQCVDFIrERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTT-DVHTVASLLKLYLRELPEPVIPFAKYEDFLSC 180
Cdd:cd04392    13 IYQLIEYL-EKNLRVEGLFRKPGNSARQQELRDLLNSGTDLDLESGGfHAHDCATVLKGFLGELPEPLLTHAHYPAHLQI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 181 AQLLSKDESEGTLELAKQVKN----------LPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDP 250
Cdd:cd04392    92 ADLCQFDEKGNKTSAPDKERLlealqlllllLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLICPRNLTP 171
                         170       180
                  ....*....|....*....|....*..
gi 1190405189 251 VTIMEGTSLVQHLMTILISKHSQLFSA 277
Cdd:cd04392   172 EDLHENAQKLNSIVTFMIKHSQKLFKA 198
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
104-250 1.49e-22

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 96.64  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 104 QCVDFIRERGLTEEGLFRMPGQ----ANLVKDLQDSFDCGeKPlFDSTTDVHTVASLLKLYLRELPEPVIPFAKYEDFLS 179
Cdd:cd04380    56 RLVDYLYTRGLAQEGLFEEPGLpsepGELLAEIRDALDTG-SP-FNSPGSAESVAEALLLFLESLPDPIIPYSLYERLLE 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190405189 180 CAQLLSKDesegtlelAKQV--KNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILRPKKEDP 250
Cdd:cd04380   134 AVANNEED--------KRQVirISLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRAG 198
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
79-252 7.06e-22

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 94.35  E-value: 7.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  79 FGQRLEDTVQyerKYG----------HRLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCG--EKPLFDS 146
Cdd:cd04397     1 FGVPLEILVE---KFGadstlgvgpgKLRIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNptEVPDLSK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 147 TTDVHtVASLLKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAkqVKNLPQANYNLLKYICKFLDEVQAHSNI 226
Cdd:cd04397    78 ENPVQ-LAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLV--YCLLPKYHRDTMEVLFSFLKWVSSFSHI 154
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1190405189 227 -----NKMSVQNLATVFGPNILRPKKEDPVT 252
Cdd:cd04397   155 deetgSKMDIHNLATVITPNILYSKTDNPNT 185
PH_RhoGap24 cd13379
Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ...
21-61 5.09e-21

Rho GTPase activating protein 24 Pleckstrin homology (PH) domain; RhoGap24 (also called ARHGAP24, p73RhoGAp, and Filamin-A-associated RhoGAP) like other RhoGAPs are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 241530  Cd Length: 114  Bit Score: 88.49  E-value: 5.09e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1190405189  21 GDREKMPVNHEAFLLMANSQNDMEDWVKAIRRVIWAPFGGG 61
Cdd:cd13379    74 GDRERMTANHETYLLMASTQNDMEDWVKSIRRVIWAPFGGG 114
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
96-258 4.77e-20

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 88.13  E-value: 4.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  96 RLAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYE 175
Cdd:cd04406    13 RSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 176 DFLSCAQLLSKDES-EGTLELAKQvknLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILR-PKKEDPVTI 253
Cdd:cd04406    93 EFLRAMGLQERRETvRGVYSVIDQ---LSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRcPDTTDPLQS 169

                  ....*
gi 1190405189 254 MEGTS 258
Cdd:cd04406   170 VQDIS 174
PH_RhoGap25-like cd13263
Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; ...
21-61 3.95e-19

Rho GTPase activating protein 25 and related proteins Pleckstrin homology (PH) domain; RhoGAP25 (also called ArhGap25) like other RhoGaps are involved in cell polarity, cell morphology and cytoskeletal organization. They act as GTPase activators for the Rac-type GTPases by converting them to an inactive GDP-bound state and control actin remodeling by inactivating Rac downstream of Rho leading to suppress leading edge protrusion and promotes cell retraction to achieve cellular polarity and are able to suppress RAC1 and CDC42 activity in vitro. Overexpression of these proteins induces cell rounding with partial or complete disruption of actin stress fibers and formation of membrane ruffles, lamellipodia, and filopodia. This hierarchy contains RhoGAP22, RhoGAP24, and RhoGAP25. Members here contain an N-terminal PH domain followed by a RhoGAP domain and either a BAR or TATA Binding Protein (TBP) Associated Factor 4 (TAF4) 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: 270083  Cd Length: 114  Bit Score: 83.20  E-value: 3.95e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1190405189  21 GDREKMPVNHEAFLLMANSQNDMEDWVKAIRRVIWAPFGGG 61
Cdd:cd13263    74 GGGDRMTSNHDSYLLMANSQAEMEEWVKVIRRVIGSPFGGG 114
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
97-255 1.08e-16

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 78.76  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  97 LAPLLVEQCVDFIRERGLTEEGLFRMPGQANLVkDLQDSFDCGEKPLFDSTTDVHTVASLLKLYLRELPEPVIPFAKYED 176
Cdd:cd04388    14 VAPPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 177 FLSCAQ-LLSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLATVFGPNILR------PKKED 249
Cdd:cd04388    93 MISRAQeVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRfqpassDSPEF 172

                  ....*.
gi 1190405189 250 PVTIME 255
Cdd:cd04388   173 HIRIIE 178
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
78-242 3.63e-16

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 77.84  E-value: 3.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  78 IFGQRLEDTVQyerKYGHRLaPLLVEQCVDFIRERGLTEEGLFRMPGQANLVKDLQDSFDC-GEKPLFDSTTdVHTVASL 156
Cdd:cd04375     4 VFGVPLLVNLQ---RTGQPL-PRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESsTDNVNYDGQQ-AYDVADM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 157 LKLYLRELPEPVIPFAKYEDFLSCAQLLSKDESEGTLELAkqVKNLPQANYNLLKYICKFLDEVQAHSNINKMSVQNLAT 236
Cdd:cd04375    79 LKQYFRDLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCA--ILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAV 156

                  ....*.
gi 1190405189 237 VFGPNI 242
Cdd:cd04375   157 CLAPSL 162
HFD_TAF4 cd08045
histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and ...
535-617 1.07e-05

histone-fold domain found in transcription initiation factor TFIID subunit 4 (TAF4) and similar proteins; TAF4, also called TATA Binding Protein (TBP) associated factor 4, RNA polymerase II TBP-associated factor subunit C, TBP-associated factor 4, transcription initiation factor TFIID 130 kDa subunit (TAF(II)130, TAFII-130, TAFII130), or transcription initiation factor TFIID 135 kDa subunit (TAF(II)135, TAFII-135, TAFII135), is a component of the TFIID complex that is composed of TATA binding protein (TBP) and a number of TBP-associated factors (TAFs). TFIID is one of the general transcription factors required for accurate and regulated initiation by RNA polymerase II. It plays a central role in mediating promoter responses to various activators and repressors. TAF4 potentiates transcriptional activation by the AF-2S of retinoic acid, vitamin D3 and thyroid hormone. TAF4 also acts as a component of the TFTC-HAT complex and some MLL1/MLL complexes. TAF4 interacts with ATF7 and the interaction inhibits ATF7-mediated transactivation.


Pssm-ID: 467027 [Multi-domain]  Cd Length: 100  Bit Score: 44.53  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 535 NNFNSMSRDSAQC-SHALQ----SLVTELkAELSKQRTEYETSLRRIeEASSSLKKQMARLEEdLDQERKKftmleiRLR 609
Cdd:cd08045    21 HGLKEVSPDVLSLlSLAVQerlrDLLEKL-IVASKHRVDSEKPDYRY-EVTSDVRRQLKALER-LEREEEE------RRR 91

                  ....*...
gi 1190405189 610 NSERARED 617
Cdd:cd08045    92 EEERERLL 99
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
551-638 1.50e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  551 LQSLVTELKAELSKQRTEYETSLRRIEEASS----SLKK------QMARLEEDLDQERKkftmleirlrnserAREDAEK 620
Cdd:pfam01576  227 LQAQIAELRAQLAKKEEELQAALARLEEETAqknnALKKireleaQISELQEDLESERA--------------ARNKAEK 292
                           90       100
                   ....*....|....*....|..
gi 1190405189  621 RNQLLQKEME----EFFSTLGT 638
Cdd:pfam01576  293 QRRDLGEELEalktELEDTLDT 314
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
146-253 2.15e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 46.17  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 146 STTDVHTVASLLKLYLRELPEPVIPFAKYEDFLScaqLLSKDESEGTLELAKQVKNLPQANYNLLKYICKFLDEVQAHSN 225
Cdd:cd04399    74 KKFEPSTVASVLKLYLLELPDSLIPHDIYDLIRS---LYSAYPPSQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFY 150
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1190405189 226 ----INKMS------VQNLATVFGPNILRPKKEDPVTI 253
Cdd:cd04399   151 rlieITKMGeseeeyADKLATSLSREILRPIIESLLTI 188
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
548-632 3.40e-05

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 43.78  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 548 SHALQSLvTELKAELSKQRTEYETslrrIEEASSSLKKQMARLEEDLDQERKkftMLEIRLRNSERAREDAEKRNQLLQK 627
Cdd:pfam07926  53 AEDIKAL-QALREELNELKAEIAE----LKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQNKLLHD 124

                  ....*
gi 1190405189 628 EMEEF 632
Cdd:pfam07926 125 QLESL 129
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
549-632 6.23e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 549 HALQSLVTELkAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERARE---------DAE 619
Cdd:COG1579    24 HRLKELPAEL-AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealqkeieSLK 102
                          90
                  ....*....|...
gi 1190405189 620 KRNQLLQKEMEEF 632
Cdd:COG1579   103 RRISDLEDEILEL 115
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
550-631 1.77e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 41.42  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAeLSKQRTEYETSLRRIEEASSSLKKQMARLEEdLDQERKKFTM----LEIRLRNS----ERAREDAEKR 621
Cdd:pfam18595  27 ALQVVEKDLRS-CIKLLEEIEAELAKLEEAKKKLKELRDALEE-KEIELRELERreerLQRQLENAqeklERLREQAEEK 104
                          90
                  ....*....|
gi 1190405189 622 NQLLQKEMEE 631
Cdd:pfam18595 105 REAAQARLEE 114
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
550-631 1.98e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEyetsLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQKEM 629
Cdd:COG4372    42 KLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                  ..
gi 1190405189 630 EE 631
Cdd:COG4372   118 EE 119
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
559-632 2.66e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 41.06  E-value: 2.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190405189 559 KAElsKQRTEYETSLRRIEEassslkkQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQKEMEEF 632
Cdd:pfam20492   3 EAE--REKQELEERLKQYEE-------ETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERL 67
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
548-631 6.04e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 6.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  548 SHALQSLVTELKAELSKQRTEYETSLRRIEEASSSLKKQMARL-EEDLDQERKKFTMLEIRLRNSER-AREDAEKRNQLL 625
Cdd:smart00935  13 SPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRKQQkLQQDLQKRQQEE 92

                   ....*.
gi 1190405189  626 QKEMEE 631
Cdd:smart00935  93 LQKILD 98
THOC7 pfam05615
Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export ...
539-621 6.65e-04

Tho complex subunit 7; The Tho complex is involved in transcription elongation and mRNA export from the nucleus.


Pssm-ID: 461692 [Multi-domain]  Cd Length: 135  Bit Score: 40.33  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 539 SMSRDSAQCSHALQSLVTELKAElSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQE------RKKFTmLEIRLRNSE 612
Cdd:pfam05615  48 DLLLDLAAFELSIEKSQLLAEAN-ERERENYEAEKEEIEEEIEAVREEIEELKERLEEAkrtrknREEYD-ALAEKINEN 125

                  ....*....
gi 1190405189 613 RAREDAEKR 621
Cdd:pfam05615 126 PSREETEKQ 134
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
559-621 7.31e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.59  E-value: 7.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1190405189 559 KAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLrNSERAREDAEKR 621
Cdd:pfam04012  92 KKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARL-KAAKAQEAVQTS 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
551-636 1.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 551 LQSLVTELK--AELSKQRTEYETSLRRIEEASSSLKKQMARL----EEDLD---QERKKFTMLEIRLRNSERAREDAEKR 621
Cdd:PRK03918  541 IKSLKKELEklEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEerlKELEPFYNEYLELKDAEKELEREEKE 620
                          90
                  ....*....|....*
gi 1190405189 622 NQLLQKEMEEFFSTL 636
Cdd:PRK03918  621 LKKLEEELDKAFEEL 635
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
550-631 1.48e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEyetsLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQKEM 629
Cdd:COG1196   243 ELEAELEELEAELEELEAE----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318

                  ..
gi 1190405189 630 EE 631
Cdd:COG1196   319 EE 320
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
548-636 1.53e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.48  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 548 SHALQSLVTELKAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERARED--AEKRNQLL 625
Cdd:pfam03938  14 SPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQelQKKQQELL 93
                          90
                  ....*....|.
gi 1190405189 626 QKEMEEFFSTL 636
Cdd:pfam03938  94 QPIQDKINKAI 104
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
550-631 2.27e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEYETSLRRIEEASSS---LKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQ 626
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336

                  ....*
gi 1190405189 627 KEMEE 631
Cdd:COG1196   337 EELEE 341
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
550-631 2.30e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 38.70  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEYETSLRRIEEassSLKKQMARLEEDLD-------QERKKFTMLEIRLRNSERAREDAEKRN 622
Cdd:pfam12474  41 LEQRQTQELRRLPKRIRAEQKKRLKMFRE---SLKQEKKELKQEVEklpkfqrKEAKRQRKEELELEQKHEELEFLQAQS 117

                  ....*....
gi 1190405189 623 QLLQKEMEE 631
Cdd:pfam12474 118 EALERELQQ 126
PRK12704 PRK12704
phosphodiesterase; Provisional
556-631 2.50e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190405189 556 TELKAELSKQRTEYETSLRRIEEASSSLKKQMARL---EEDLDQERKKftmLEIRLRNSERAREDAEKRNQLLQKEMEE 631
Cdd:PRK12704   71 NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLekrEEELEKKEKE---LEQKQQELEKKEEELEELIEEQLQELER 146
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
557-631 2.59e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.87  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 557 ELKAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERK---KFTMLEIRLRNSE---RAREDAEK----RNQLLQ 626
Cdd:pfam05672  47 ELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREqreQEEQERLQKQKEEaeaKAREEAERqrqeREKIMQ 126

                  ....*
gi 1190405189 627 KEMEE 631
Cdd:pfam05672 127 QEEQE 131
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
554-631 2.80e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 38.88  E-value: 2.80e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1190405189 554 LVTELKAELSKQRTEYETS-LRRIEEASSSLKKQMarlEEDLDQERkkftmlEIRLRNSERAREDAEKRNQLLQKEMEE 631
Cdd:pfam15346  20 VAKRVEEELEKRKDEIEAEvERRVEEARKIMEKQV---LEELERER------EAELEEERRKEEEERKKREELERILEE 89
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
511-630 3.29e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.93  E-value: 3.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  511 AELGDSSERLAVCVSTLNG--SGSEGNNFNSmSRDSAQCSHALQSlVTELKAELSKQRTEYETSLRRIEEASSSLKKQMA 588
Cdd:pfam01576  429 AELAEKLSKLQSELESVSSllNEAEGKNIKL-SKDVSSLESQLQD-TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1190405189  589 RLEEDLDQERKKFTMLEIRLRNSERARED-------AEKRNQLLQKEME 630
Cdd:pfam01576  507 EEEEAKRNVERQLSTLQAQLSDMKKKLEEdagtleaLEEGKKRLQRELE 555
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
550-631 3.42e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEYETSLRRIEEasssLKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQKEM 629
Cdd:COG4372    91 AAQAELAQAQEELESLQEEAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166

                  ..
gi 1190405189 630 EE 631
Cdd:COG4372   167 AA 168
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
558-631 3.99e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.32  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 558 LKAELSKQR-TEYETSLRRIEEASSSLKKQMAR---LEEDLDQERKKFTMlEIRLRNS----ERAREDAEKRNQLLQKEM 629
Cdd:pfam15709 338 LRAERAEMRrLEVERKRREQEEQRRLQQEQLERaekMREELELEQQRRFE-EIRLRKQrleeERQRQEEEERKQRLQLQA 416

                  ..
gi 1190405189 630 EE 631
Cdd:pfam15709 417 AQ 418
RhoGAP_fMSB1 cd04401
RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
148-240 4.21e-03

RhoGAP_fMSB1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal MSB1-like proteins. Msb1 was originally identified as a multicopy suppressor of temperature sensitive cdc42 mutation. Msb1 is a positive regulator of the Pkc1p-MAPK pathway and 1,3-beta-glucan synthesis, both pathways involve Rho1 regulation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239866  Cd Length: 198  Bit Score: 38.87  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 148 TDVHTVASLLKLYLRELPEPVIPFAK-YEDFlsCAQllskdESEGT------LELAKQVknLPQANYNLLKYicKFLD-- 218
Cdd:cd04401    68 ADPHTLILVLKWIWSRLPGSKVIWWEvYEEF--KAR-----ERRSNypadafLDLLPQC--LSSPAHASILY--DFFDll 136
                          90       100
                  ....*....|....*....|...
gi 1190405189 219 -EVQAHSNINKMSVQNLATVFGP 240
Cdd:cd04401   137 sSIAAHSSVNGMSGRKLSKMAGP 159
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
539-640 5.14e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 39.67  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 539 SMSRDSAQCSHALQSLVTELkAELSKQRTEYETSLRRIEEASSSLK-------KQMARLEEDLDQE-------------- 597
Cdd:pfam19220  66 KLRRELAGLTRRLSAAEGEL-EELVARLAKLEAALREAEAAKEELRielrdktAQAEALERQLAAEteqnraleeenkal 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1190405189 598 RKKFTMLEIRLRNSERAREDAEKRNQL-------LQKEMEEFFSTLGTLT 640
Cdd:pfam19220 145 REEAQAAEKALQRAEGELATARERLALleqenrrLQALSEEQAAELAELT 194
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
557-639 5.47e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 557 ELKAELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLdQERKKFTM-LEIRLRNSERAREDAEKRNQLLQKEMEEFFST 635
Cdd:pfam13863  10 LVQLALDAKREEIERLEELLKQREEELEKKEQELKEDL-IKFDKFLKeNDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88

                  ....
gi 1190405189 636 LGTL 639
Cdd:pfam13863  89 IEEL 92
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
550-631 5.58e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEYETSLRRIEEASSSLK-----KQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQL 624
Cdd:COG1579    49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128

                  ....*..
gi 1190405189 625 LQKEMEE 631
Cdd:COG1579   129 LEAELAE 135
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
510-632 5.73e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 38.88  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 510 LAELGDSSERLAVCVSTlnGSGSEGNNFNSMSRDSAQCSHALQSLVTELKAELS-----------------KQRTEYETS 572
Cdd:cd07596    41 LGEFGKALIKLAKCEEE--VGGELGEALSKLGKAAEELSSLSEAQANQELVKLLeplkeylrycqavketlDDRADALLT 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1190405189 573 LRRIEEASSSLKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKR----NQLLQKEMEEF 632
Cdd:cd07596   119 LQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEARKRyeeiSERLKEELKRF 182
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
550-631 5.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 550 ALQSLVTELKAELSKQRTEYETSLRRIEEasssLKKQMARLEEDLDQERKKFTMLEIRLRNSERAREDAEKRNQLLQKEM 629
Cdd:COG4372    49 QLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124

                  ..
gi 1190405189 630 EE 631
Cdd:COG4372   125 QD 126
PRK14143 PRK14143
heat shock protein GrpE; Provisional
499-615 6.49e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237624 [Multi-domain]  Cd Length: 238  Bit Score: 38.56  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 499 QGSPAASSDIKLAELGDSSERLAVCVSTLNGSGSEGNNFNSMSRDSAQCSHALQSLVTELKAELSKQRTEYET---SLRR 575
Cdd:PRK14143   13 AVISESEAEDNSPESSEEVTEQEAELTNPEGDAAEAESSPDSGSAASETAADNAARLAQLEQELESLKQELEElnsQYMR 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1190405189 576 IEEASSSLKKQMARLEEDLDQERKKFTMLEIR--LRNSERAR 615
Cdd:PRK14143   93 IAADFDNFRKRTSREQEDLRLQLKCNTLSEILpvVDNFERAR 134
PH1_PLEKHH1_PLEKHH2 cd13282
Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 ...
33-54 6.80e-03

Pleckstrin homology (PH) domain containing, family H (with MyTH4 domain) members 1 and 2 (PLEKHH1) PH domain, repeat 1; PLEKHH1 and PLEKHH2 (also called PLEKHH1L) are thought to function in phospholipid binding and signal transduction. There are 3 Human PLEKHH genes: PLEKHH1, PLEKHH2, and PLEKHH3. There are many isoforms, the longest of which contain a FERM domain, a MyTH4 domain, two PH domains, a peroximal domain, a vacuolar domain, and a coiled coil stretch. The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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: 241436  Cd Length: 96  Bit Score: 36.51  E-value: 6.80e-03
                          10        20
                  ....*....|....*....|..
gi 1190405189  33 FLLMANSQNDMEDWVKAIRRVI 54
Cdd:cd13282    70 YYLTADSENDLDEWIRVIQNVL 91
PH pfam00169
PH domain; PH stands for pleckstrin homology.
29-54 6.89e-03

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 36.77  E-value: 6.89e-03
                          10        20
                  ....*....|....*....|....*.
gi 1190405189  29 NHEAFLLMANSQNDMEDWVKAIRRVI 54
Cdd:pfam00169  79 GKRTYLLQAESEEERKDWIKAIQSAI 104
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
539-632 7.15e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189  539 SMSRDSAQCSHALQSLVTELKaELSKQRTEYETSLRRIEEASSSLKKQMARLEEDLDQERK-------KFTMLEIRLRNS 611
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleelsrQISALRKDLARL 738
                           90       100
                   ....*....|....*....|.
gi 1190405189  612 ERAREDAEKRNQLLQKEMEEF 632
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTEL 759
FliJ pfam02050
Flagellar FliJ protein;
538-634 8.39e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 36.88  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1190405189 538 NSMSRDSAQCSHALQSLVTELKAELSKQRTEYETSLRRIEEASSSLKKQMarleedldQERKKFTMLEIRLRNSERAred 617
Cdd:pfam02050  37 GAGQGISAAELRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREEWQEAR--------QERKSLEKLREREKKEERK--- 105
                          90
                  ....*....|....*..
gi 1190405189 618 AEKRNQllQKEMEEFFS 634
Cdd:pfam02050 106 EQNRRE--QKQLDELAA 120
 
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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