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Conserved domains on  [gi|1227107233|gb|OXU29741.1|]
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hypothetical protein TSAR_012326 [Trichomalopsis sarcophagae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.05e-70

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


:

Pssm-ID: 269995  Cd Length: 118  Bit Score: 231.53  E-value: 3.05e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13174     81 WGGMNYAEDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1364 8.19e-66

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


:

Pssm-ID: 269992  Cd Length: 117  Bit Score: 218.88  E-value: 8.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIWV 1327
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDKEWKERGIGNLKILKNPAtGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYIWA 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1328 ANDFADEELRLEKLCIKFKTVEEAASFKENFEKAKDS 1364
Cdd:cd13171     81 ANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1944-2060 3.75e-63

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 cd13173:

Pssm-ID: 473070  Cd Length: 115  Bit Score: 211.19  E-value: 3.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDsaTKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWMWT 2023
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFV--DKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSWMWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2024 AGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNACSG 2060
Cdd:cd13173     79 AHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 2764-2867 1.18e-30

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 cd13175:

Pssm-ID: 473070  Cd Length: 114  Bit Score: 118.02  E-value: 1.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNNE-LASETVISVDTTMQYNEKECTWAAIDYAVEPQ 2842
Cdd:cd13175      9 MFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDtIIANTIIAVQTSLRVEGKEAIWSAIDYSQEPL 88

                           90       100
                   ....*....|....*....|....*
gi 1227107233 2843 VRRTLRAVFSSSQTAEQMYQTFQEG 2867
Cdd:cd13175     89 LRRRFRAEFSSDDAAQEFSVVFNEG 113
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1509-1616 1.01e-14

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 pfam00638:

Pssm-ID: 473070 [Multi-domain]  Cd Length: 122  Bit Score: 72.85  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYN-QIVPPRTVFNLKSDTV 1587
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANhYITPDMTLKPLAGSDR 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 1588 NWT-----IENEKNKPDSYLARFKNYDQASLFQK 1616
Cdd:pfam00638   81 SWVwtaadFADGEGKPEQLAIRFKTKEEADSFKK 114
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 2367-2467 7.28e-09

Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.


:

Pssm-ID: 463941 [Multi-domain]  Cd Length: 90  Bit Score: 54.93  E-value: 7.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2367 SIFG-TTTTITSLFGGTASTLPS----FGALANQGNTTANGGLFSSNTFGSTTPALDAKSTTVSAPASttttttvGSTIF 2441
Cdd:pfam13634    1 GLFGaATSTSGGLFGNTSTTAASggglFGAASTATATTSGGGLFGNSSSNAPSGGLFGATNTTTQTAT-------GGGLF 73

                           90       100
                   ....*....|....*....|....*.
gi 1227107233 2442 GGNAATQFTskltfgtgvAPTTNVFG 2467
Cdd:pfam13634   74 GNNAATTTS---------TTGGGLFG 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-140 7.44e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 53.66  E-value: 7.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLAdpEV 108
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALElDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL--KA 85

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233  109 GiDVNRAKYWVDRADKLFPPHKSVFQLKEKIL 140
Cdd:COG4783     86 G-DYDEALALLEKALKLDPEHPEAYLRLARAY 116
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1655-1679 2.33e-06

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 46.16  E-value: 2.33e-06
                            10        20
                    ....*....|....*....|....*
gi 1227107233  1655 GSWECKGCYMRNSASAKSCVACQAP 1679
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1711-1739 8.40e-05

Zn-finger in Ran binding protein and others;


:

Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 41.57  E-value: 8.40e-05
                           10        20
                   ....*....|....*....|....*....
gi 1227107233 1711 AGSWECKDCYTRNDAGVTKCVACQAAAPG 1739
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPKPD 30
PEP_TPR_lipo super family cl37187
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 59-307 1.29e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


The actual alignment was detected with superfamily member TIGR02917:

Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 47.77  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   59 PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQeeliLKVCELLADpeVGIDVNRAKYWVDRADKLFPPHKSVFQLKEK 138
Cdd:TIGR02917  465 ASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDF----FPAAANLAR--IDIQEGNPDDAIQRFEKVLTIDPKNLRAILA 538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  139 ILSIERPTNNQEDLENLITAELATRPTDVHLRVKLIKHYMERSKLDEAYkhATDIEASSIHRDSVIWYQVLCELFLKCKy 218
Cdd:TIGR02917  539 LAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL--AILNEAADAAPDSPEAWLMLGRAQLAAG- 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  219 NHQtmwsfwiSYISALERYAALsLKEQGSSVRKTSEAIQAVYNFDQHLFEAKgQSFSSYPSLTESIFVhmwgqlhfhLAC 298
Cdd:TIGR02917  616 DLN-------KAVSSFKKLLAL-QPDSALALLLLADAYAVMKNYAKAITSLK-RALELKPDNTEAQIG---------LAQ 677


                   ....*....
gi 1227107233  299 LLIQNTQRE 307
Cdd:TIGR02917  678 LLLAAKRTE 686
IR1-M super family cl13601
Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...
 2086-2133 4.94e-04

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00638, pfam00641, pfam00160. There are two conserved sequence motifs: TFFC and EDF. Nup358/RanBP2 is a nucleoporin involved in ubiquitination of many different protein targets from various cellular pathways. It complexes with Ubc9, SUMO-1 and RanGAP1 to perform this function. This is the ligase domain which binds to Ubc9.


The actual alignment was detected with superfamily member pfam12185:

Pssm-ID: 463488  Cd Length: 60  Bit Score: 40.53  E-value: 4.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1227107233 2086 DIEVVYEIKVTPEEKAAALKLKLPENFYsykyksdcpgCRGCKDSDES 2133
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFF----------CGYSSDTDDG 38
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1768-1790 3.56e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 3.56e-03
                            10        20
                    ....*....|....*....|...
gi 1227107233  1768 GSWECKQCYVVNSQSNQYCAACD 1790
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23
 
Name Accession Description Interval E-value
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.05e-70

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 231.53  E-value: 3.05e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13174     81 WGGMNYAEDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1364 8.19e-66

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 269992  Cd Length: 117  Bit Score: 218.88  E-value: 8.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIWV 1327
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDKEWKERGIGNLKILKNPAtGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYIWA 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1328 ANDFADEELRLEKLCIKFKTVEEAASFKENFEKAKDS 1364
Cdd:cd13171     81 ANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2060 3.75e-63

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy.


Pssm-ID: 269994  Cd Length: 115  Bit Score: 211.19  E-value: 3.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDsaTKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWMWT 2023
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFV--DKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSWMWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2024 AGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNACSG 2060
Cdd:cd13173     79 AHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1235-1361 5.18e-48

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 168.33  E-value: 5.18e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1235 FAPIIPLPDeVPVTTGEENEEELYCARAKLFRFVD--KEWKERGIGNVKLLKNTE--GKIRLLMRREQVLKICANHMLRK 1310
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANdkKEWKERGVGDLKILKSKDngGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1227107233  1311 DMELTMMKNNEKAYIWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKA 1361
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1941-2057 7.60e-47

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 164.52  E-value: 7.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1941 EVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDK 2018
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKplAGSDR 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 2019 TWMWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEA 119
Ran_BP1 pfam00638
RanBP1 domain;
1247-1362 9.78e-47

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 164.52  E-value: 9.78e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1247 VTTGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKA 1323
Cdd:pfam00638    2 VKTGEEDEEVLFSQRAKLFRFdaEVKQWKERGVGDIKILKNKDdGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDRS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 1324 YIWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:pfam00638   82 WVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQ 120
Ran_BP1 pfam00638
RanBP1 domain;
2593-2715 4.35e-46

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 162.60  E-value: 4.35e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2593 EVRTGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDR 2672
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1227107233 2673 AWMWAGMNYAEADsPEVEQLAVRFKTPELASQFKEAVDKAQQA 2715
Cdd:pfam00638   81 SWVWTAADFADGE-GKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 2582-2712 7.19e-46

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 162.17  E-value: 7.19e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  2582 FEPIIPLPDaIEVRTGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGT-YRLLLRREQVHKVVCNLLLTS 2660
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGGkVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1227107233  2661 DLEFRELNSSDRAWMWAGMNYAEaDSPEVEQLAVRFKTPELASQFKEAVDKA 2712
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFAD-DIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1930-2057 1.69e-45

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 161.02  E-value: 1.69e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1930 FAPVIPLPDkIEVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVE-TKKLRLVMRRDQVLKLCLNHAVTP 2008
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDnGGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1227107233  2009 ALEISSKD--DKTWMWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:smart00160   80 SMTLKPLAgsNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1918-2057 9.52e-39

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 145.16  E-value: 9.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1918 DEDVVEEAEDVYFAPVIPLpDKIEVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQV 1997
Cdd:COG5171     59 DEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKT 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1227107233 1998 LKLCLNHAVTP--ALEISSKDDKTWMWT-AGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:COG5171    138 LKLCANHFINPefKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKG 200
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
2516-2714 5.23e-31

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 122.82  E-value: 5.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2516 EQKPAFKTDPNFTfegaGASVFGVKNAQKTGDKTKKTPNSKKDKAKDDDDEDGDDEnengdehDPYFEPIIPLpDAIEVR 2595
Cdd:COG5171     16 ENEQKERSLDVVS----KGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKGPESP-------NIHFEPVVEL-QRVHLK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:COG5171     84 TNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWV 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1227107233 2676 WA-GMNYAEADsPEVEQLAVRFKTPELASQFKEAVDKAQQ 2714
Cdd:COG5171    164 WMsTADTVEGE-AKAQTFAIRFYSEENAKRFKEEFEKGQE 202
RanBD5_RanBP2_insect-like cd13175
Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ...
 2764-2867 1.18e-30

Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 5 is present in this hierarchy.


Pssm-ID: 269996  Cd Length: 114  Bit Score: 118.02  E-value: 1.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNNE-LASETVISVDTTMQYNEKECTWAAIDYAVEPQ 2842
Cdd:cd13175      9 MFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDtIIANTIIAVQTSLRVEGKEAIWSAIDYSQEPL 88

                           90       100
                   ....*....|....*....|....*
gi 1227107233 2843 VRRTLRAVFSSSQTAEQMYQTFQEG 2867
Cdd:cd13175     89 LRRRFRAEFSSDDAAQEFSVVFNEG 113
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1203-1377 1.50e-29

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 118.58  E-value: 1.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1203 KPQDNQNSSLLSTGSRHSSSDVTEVEHDPIpDFAPIIPLpDEVPVTTGEENEEELYCARAKLFRFVD--KEWKERGIGNV 1280
Cdd:COG5171     40 GEEKKVQQSPFLENAVPEGDEGKGPESPNI-HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEeaKEWKERGTGDM 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1281 KLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIW-VANDFADEELRLEKLCIKFKTVEEAASFKENF 1358
Cdd:COG5171    118 IILKHKKtNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWmSTADTVEGEAKAQTFAIRFYSEENAKRFKEEF 197

                          170
                   ....*....|....*....
gi 1227107233 1359 EKAKdslpdEEAKPATETK 1377
Cdd:COG5171    198 EKGQ-----EHNEKALKTK 211
Ran_BP1 pfam00638
RanBP1 domain;
1509-1616 1.01e-14

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 72.85  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYN-QIVPPRTVFNLKSDTV 1587
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANhYITPDMTLKPLAGSDR 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 1588 NWT-----IENEKNKPDSYLARFKNYDQASLFQK 1616
Cdd:pfam00638   81 SWVwtaadFADGEGKPEQLAIRFKTKEEADSFKK 114
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1514-1618 2.71e-14

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 71.47  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPR---TVFNLKSDTVNWT 1590
Cdd:cd00835      3 EENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDmklTKMGNNDRAWVWT 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233 1591 I----ENEKNKPDSYLARFKNYDQASLFQKSL 1618
Cdd:cd00835     83 AmddsEDGEGKPETFAVRFKTAEDAEEFKKAF 114
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1505-1616 2.48e-11

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 63.56  E-value: 2.48e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1505 SKGSEVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEK-STGRVRLLMNTEDNSKTIYN-QIVPPRTVFNL 1582
Cdd:smart00160    7 LPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANhPIFKSMTLKPL 86

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1227107233  1583 KSDTVNWTIENEKN-----KPDSYLARFKNYDQASLFQK 1616
Cdd:smart00160   87 AGSNRALKWTPEDFaddipKLVLYAVRFKTKEEADSFKN 125
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 2367-2467 7.28e-09

Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.


Pssm-ID: 463941 [Multi-domain]  Cd Length: 90  Bit Score: 54.93  E-value: 7.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2367 SIFG-TTTTITSLFGGTASTLPS----FGALANQGNTTANGGLFSSNTFGSTTPALDAKSTTVSAPASttttttvGSTIF 2441
Cdd:pfam13634    1 GLFGaATSTSGGLFGNTSTTAASggglFGAASTATATTSGGGLFGNSSSNAPSGGLFGATNTTTQTAT-------GGGLF 73

                           90       100
                   ....*....|....*....|....*.
gi 1227107233 2442 GGNAATQFTskltfgtgvAPTTNVFG 2467
Cdd:pfam13634   74 GNNAATTTS---------TTGGGLFG 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-140 7.44e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 53.66  E-value: 7.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLAdpEV 108
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALElDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL--KA 85

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233  109 GiDVNRAKYWVDRADKLFPPHKSVFQLKEKIL 140
Cdd:COG4783     86 G-DYDEALALLEKALKLDPEHPEAYLRLARAY 116
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1655-1679 2.33e-06

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 46.16  E-value: 2.33e-06
                            10        20
                    ....*....|....*....|....*
gi 1227107233  1655 GSWECKGCYMRNSASAKSCVACQAP 1679
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1654-1682 7.67e-06

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 44.65  E-value: 7.67e-06
                           10        20
                   ....*....|....*....|....*....
gi 1227107233 1654 AGSWECKGCYMRNSASAKSCVACQAPSPS 1682
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPKPD 30
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1509-1627 1.17e-05

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 48.86  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVF--NLKSDT 1586
Cdd:COG5171     81 HLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLqpNVGSDR 160

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1227107233 1587 vNW-------TIENEKnKPDSYLARFKNYDQASLFQKSLMGYLEKSAK 1627
Cdd:COG5171    161 -SWvwmstadTVEGEA-KAQTFAIRFYSEENAKRFKEEFEKGQEHNEK 206
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1711-1739 8.40e-05

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 41.57  E-value: 8.40e-05
                           10        20
                   ....*....|....*....|....*....
gi 1227107233 1711 AGSWECKDCYTRNDAGVTKCVACQAAAPG 1739
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPKPD 30
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 59-307 1.29e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 47.77  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   59 PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQeeliLKVCELLADpeVGIDVNRAKYWVDRADKLFPPHKSVFQLKEK 138
Cdd:TIGR02917  465 ASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDF----FPAAANLAR--IDIQEGNPDDAIQRFEKVLTIDPKNLRAILA 538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  139 ILSIERPTNNQEDLENLITAELATRPTDVHLRVKLIKHYMERSKLDEAYkhATDIEASSIHRDSVIWYQVLCELFLKCKy 218
Cdd:TIGR02917  539 LAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL--AILNEAADAAPDSPEAWLMLGRAQLAAG- 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  219 NHQtmwsfwiSYISALERYAALsLKEQGSSVRKTSEAIQAVYNFDQHLFEAKgQSFSSYPSLTESIFVhmwgqlhfhLAC 298
Cdd:TIGR02917  616 DLN-------KAVSSFKKLLAL-QPDSALALLLLADAYAVMKNYAKAITSLK-RALELKPDNTEAQIG---------LAQ 677


                   ....*....
gi 1227107233  299 LLIQNTQRE 307
Cdd:TIGR02917  678 LLLAAKRTE 686
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1712-1735 2.70e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 40.38  E-value: 2.70e-04
                            10        20
                    ....*....|....*....|....
gi 1227107233  1712 GSWECKDCYTRNDAGVTKCVACQA 1735
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGA 24
IR1-M pfam12185
Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...
 2086-2133 4.94e-04

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00638, pfam00641, pfam00160. There are two conserved sequence motifs: TFFC and EDF. Nup358/RanBP2 is a nucleoporin involved in ubiquitination of many different protein targets from various cellular pathways. It complexes with Ubc9, SUMO-1 and RanGAP1 to perform this function. This is the ligase domain which binds to Ubc9.


Pssm-ID: 463488  Cd Length: 60  Bit Score: 40.53  E-value: 4.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1227107233 2086 DIEVVYEIKVTPEEKAAALKLKLPENFYsykyksdcpgCRGCKDSDES 2133
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFF----------CGYSSDTDDG 38
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 2367-2487 1.93e-03

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 43.99  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2367 SIFGTTTTITSLFGGTASTLPSFGALANQGNTTANGGLFSSNTFGSTTPALDAKSTTVSApASTTTTTTVGSTIFGGNAA 2446
Cdd:COG3210    813 NVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAA-TAASITVGSGGVATSTGTA 891

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1227107233 2447 TQFTSKLTFGTGVAPTTNVFGNLSSGTSNIFGGSKPSIGDS 2487
Cdd:COG3210    892 NAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAA 932
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1768-1790 3.56e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 3.56e-03
                            10        20
                    ....*....|....*....|...
gi 1227107233  1768 GSWECKQCYVVNSQSNQYCAACD 1790
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1767-1793 4.06e-03

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 36.95  E-value: 4.06e-03
                           10        20
                   ....*....|....*....|....*..
gi 1227107233 1767 AGSWECKQCYVVNSQSNQYCAACDKAK 1793
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPK 28
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 33-90 4.50e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 41.85  E-value: 4.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1227107233   33 AELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEP 90
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALElEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
PRK12688 PRK12688
flagellin; Reviewed
 2370-2480 7.14e-03

flagellin; Reviewed


Pssm-ID: 171664 [Multi-domain]  Cd Length: 751  Bit Score: 41.79  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2370 GTTTTITS--LFGGTASTLPSFGALANQGNTTANGGLFSSNTFGSTTPALDAKSTtvsaPASTTTTTTVGSTIfggnaat 2447
Cdd:PRK12688   145 GGATAATGatTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTTATGLLGNAQ----PADGDTLTVNGKTI------- 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1227107233 2448 qftsklTFGTGVAPTT-------NVFGNL---SSGTSNIFGGS 2480
Cdd:PRK12688   214 ------TFRSGAAPAStavpsgsGVSGNLvtdGNGNSTVYLGS 250
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 30-85 9.70e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 36.93  E-value: 9.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLM---GQILEALGQKEAAVVQYKRA 85
Cdd:pfam13432    1 LALARAALRAGDYDDAAAALEAALArFPESPDAAAALlllGLAALRQGRLAEAAAAYRAA 60
 
Name Accession Description Interval E-value
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.05e-70

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 231.53  E-value: 3.05e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13174     81 WGGMNYAEDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1364 8.19e-66

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 269992  Cd Length: 117  Bit Score: 218.88  E-value: 8.19e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIWV 1327
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDKEWKERGIGNLKILKNPAtGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYIWA 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1328 ANDFADEELRLEKLCIKFKTVEEAASFKENFEKAKDS 1364
Cdd:cd13171     81 ANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2060 3.75e-63

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy.


Pssm-ID: 269994  Cd Length: 115  Bit Score: 211.19  E-value: 3.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDsaTKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWMWT 2023
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFV--DKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSWMWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2024 AGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNACSG 2060
Cdd:cd13173     79 AHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1233-1362 1.23e-55

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270000 [Multi-domain]  Cd Length: 136  Bit Score: 190.47  E-value: 1.23e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1233 PDFAPIIPLPdEVPVTTGEENEEELYCARAKLFRFVD----KEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHM 1307
Cdd:cd13179      2 AQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTendpPEWKERGTGDVKLLKHKEtKKIRLLMRRDKTLKICANHY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1227107233 1308 LRKDMELTMMKNNEKAYIWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13179     81 ITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 2596-2713 1.47e-54

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 186.65  E-value: 1.47e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd00835     81 WTAMDDSEDGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1944-2058 3.07e-54

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 185.49  E-value: 3.07e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTWM 2021
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTkmGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2022 WTAGDYSE-GEIEYMQFACRFKTPEIAADFKNAVDNAC 2058
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1944-2057 1.29e-53

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 183.63  E-value: 1.29e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTWM 2021
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKpnAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEA 116
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 2596-2713 1.17e-52

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 180.94  E-value: 1.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEaDSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13176     81 WTALDFSE-EEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1249-1362 3.29e-52

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 179.78  E-value: 3.29e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFvDKE---WKERGIGNVKLLKN-TEGKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAY 1324
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRF-DKDvkqWKERGVGDIKILQHkTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSW 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 1325 IWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13176     80 VWTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1249-1362 7.57e-52

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 178.94  E-value: 7.57e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVD--KEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYI 1325
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKetKEWKERGVGDLKILKNKDtGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 1326 WVANDFAD-EELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1927-2058 2.52e-51

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270000 [Multi-domain]  Cd Length: 136  Bit Score: 178.15  E-value: 2.52e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1927 DVYFAPVIPLPdKIEVKTGEENEDVLYSHRAKLFKFDSA--TKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNH 2004
Cdd:cd13179      1 DAQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTEndPPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1227107233 2005 AVTPALEISSK--DDKTWMWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNAC 2058
Cdd:cd13179     80 YITPEMKLKPNagSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 2579-2714 8.16e-50

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270000 [Multi-domain]  Cd Length: 136  Bit Score: 173.52  E-value: 8.16e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2579 DPYFEPIIPLPdAIEVRTGEEDEEKVFCHRAKLYRYDN--NTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNL 2656
Cdd:cd13179      1 DAQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTenDPPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1227107233 2657 LLTSDLEFRELNSSDRAWMWAGMNYAEADsPEVEQLAVRFKTPELASQFKEAVDKAQQ 2714
Cdd:cd13179     80 YITPEMKLKPNAGSDRAWVWTCADFADEE-PKPELFAIRFANAENAQKFKEAFEEAQK 136
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1362 1.40e-48

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 169.44  E-value: 1.40e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKN-TEGKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYI 1325
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFdvETKEWKERGIGNVKILRHkTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1326 WVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1235-1361 5.18e-48

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 168.33  E-value: 5.18e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1235 FAPIIPLPDeVPVTTGEENEEELYCARAKLFRFVD--KEWKERGIGNVKLLKNTE--GKIRLLMRREQVLKICANHMLRK 1310
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANdkKEWKERGVGDLKILKSKDngGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1227107233  1311 DMELTMMKNNEKAYIWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKA 1361
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1941-2057 7.60e-47

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 164.52  E-value: 7.60e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1941 EVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDK 2018
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKplAGSDR 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 2019 TWMWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEA 119
Ran_BP1 pfam00638
RanBP1 domain;
1247-1362 9.78e-47

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 164.52  E-value: 9.78e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1247 VTTGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKA 1323
Cdd:pfam00638    2 VKTGEEDEEVLFSQRAKLFRFdaEVKQWKERGVGDIKILKNKDdGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDRS 81

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 1324 YIWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:pfam00638   82 WVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQ 120
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2057 1.18e-46

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269993  Cd Length: 118  Bit Score: 163.78  E-value: 1.18e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVE-TKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTW 2020
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKEdNNKVRLLMRREQVLKVCCNQRLTKDMEFKylTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2021 MWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKA 117
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1362 2.15e-46

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269993  Cd Length: 118  Bit Score: 163.39  E-value: 2.15e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKNTE--GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAY 1324
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFdkATKEWKERGLGNIKLLRNKEdnNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 1325 IWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.92e-46

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269993  Cd Length: 118  Bit Score: 162.62  E-value: 3.92e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEH-GTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAW 2674
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKEDnNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 2675 MWAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13172     81 TWCAQDYSEGEL-KPETFAIRFKTQEICKDFLDAVKKAQ 118
Ran_BP1 pfam00638
RanBP1 domain;
2593-2715 4.35e-46

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 162.60  E-value: 4.35e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2593 EVRTGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDR 2672
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1227107233 2673 AWMWAGMNYAEADsPEVEQLAVRFKTPELASQFKEAVDKAQQA 2715
Cdd:pfam00638   81 SWVWTAADFADGE-GKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 2582-2712 7.19e-46

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 162.17  E-value: 7.19e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  2582 FEPIIPLPDaIEVRTGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGT-YRLLLRREQVHKVVCNLLLTS 2660
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGGkVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|..
gi 1227107233  2661 DLEFRELNSSDRAWMWAGMNYAEaDSPEVEQLAVRFKTPELASQFKEAVDKA 2712
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFAD-DIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1930-2057 1.69e-45

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 161.02  E-value: 1.69e-45
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1930 FAPVIPLPDkIEVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVE-TKKLRLVMRRDQVLKLCLNHAVTP 2008
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDnGGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1227107233  2009 ALEISSKD--DKTWMWTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:smart00160   80 SMTLKPLAgsNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1364 1.63e-44

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy.


Pssm-ID: 269994  Cd Length: 115  Bit Score: 157.64  E-value: 1.63e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTmmKNNEKAYIWV 1327
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDKEWKERGLGDVKILRHKEtGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWMWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1328 ANDFADEELRLEKLCIKFKTVEEAASFKENFEKAKDS 1364
Cdd:cd13173     79 AHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2057 5.84e-42

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy.


Pssm-ID: 270204  Cd Length: 117  Bit Score: 150.50  E-value: 5.84e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTP--ALEISSKDDKTWM 2021
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITAdmKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEA 116
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1362 1.00e-41

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy.


Pssm-ID: 270204  Cd Length: 117  Bit Score: 149.73  E-value: 1.00e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFvDKE---WKERGIGNVKLLKNTEGK-IRLLMRREQVLKICANHMLRKDMELTMMKNNEKAY 1324
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRY-DKDaaqWKERGIGDLKILQNYDNKqVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAW 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 1325 IWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd14685     80 VWTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 2.03e-41

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 149.02  E-value: 2.03e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEaDSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd14684     81 WNALDYAD-ELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1362 1.27e-40

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269998 [Multi-domain]  Cd Length: 117  Bit Score: 146.73  E-value: 1.27e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKN-TEGKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYI 1325
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFdaSVSQWKERGVGNLKILKNaVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1326 WVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2056 9.52e-40

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269998 [Multi-domain]  Cd Length: 117  Bit Score: 144.03  E-value: 9.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTWM 2021
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKplAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDN 2056
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEE 115
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2712 5.94e-39

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy.


Pssm-ID: 269994  Cd Length: 115  Bit Score: 141.85  E-value: 5.94e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYdnNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRElnSSDRAWM 2675
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRF--VDKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2676 WAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKA 2712
Cdd:cd13173     77 WAAHDFSEGES-ELERFAIRFKNAEIAQGFMKAIDDA 112
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1918-2057 9.52e-39

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 145.16  E-value: 9.52e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1918 DEDVVEEAEDVYFAPVIPLpDKIEVKTGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQV 1997
Cdd:COG5171     59 DEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKT 137

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1227107233 1998 LKLCLNHAVTP--ALEISSKDDKTWMWT-AGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:COG5171    138 LKLCANHFINPefKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKG 200
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2057 1.32e-38

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 141.00  E-value: 1.32e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTWM 2021
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRpmNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 2022 WTAGDYSE---GEIEymQFACRFKTPEIAADFKNAVDNA 2057
Cdd:cd13174     81 WGGMNYAEdaePEVE--TLAVRFKNEEIASQFKNVVDQC 117
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2057 3.39e-38

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 139.78  E-value: 3.39e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEI--SSKDDKTWM 2021
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLkpNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNA 2057
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEA 116
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 4.05e-38

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy.


Pssm-ID: 270204  Cd Length: 117  Bit Score: 139.72  E-value: 4.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd14685     81 WTAMDFAEGEG-KIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2060 4.12e-38

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 269992  Cd Length: 117  Bit Score: 139.52  E-value: 4.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFdsATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISS--KDDKTWM 2021
Cdd:cd13171      1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPmkKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKNAVDNACSG 2060
Cdd:cd13171     79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.17e-37

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269999  Cd Length: 117  Bit Score: 137.01  E-value: 3.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13178     81 WTATDYADGEG-KVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2713 3.75e-37

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269998 [Multi-domain]  Cd Length: 117  Bit Score: 136.72  E-value: 3.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13177     81 WMANDFSDGDA-KLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 2596-2715 1.88e-36

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 269992  Cd Length: 117  Bit Score: 134.90  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYdnNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:cd13171      1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1227107233 2676 WAGMNYAEADSpEVEQLAVRFKTPELASQFKEAVDKAQQA 2715
Cdd:cd13171     79 WAANDFADEVV-VLEKLCVRFKTVELAKEFRDVFTKAKKE 117
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1944-2052 2.55e-36

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269999  Cd Length: 117  Bit Score: 134.31  E-value: 2.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEIS--SKDDKTWM 2021
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQplSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1227107233 2022 WTAGDYSEGEIEYMQFACRFKTPEIAADFKN 2052
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKK 111
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1362 8.71e-35

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269999  Cd Length: 117  Bit Score: 130.07  E-value: 8.71e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFvDK---EWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAY 1324
Cdd:cd13178      1 SGEEDEEILFKERAKLYRW-DRdvgQWKERGVGDIKILFHPSkHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 1325 IWVANDFADEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13178     80 VWTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1249-1361 7.00e-32

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 121.75  E-value: 7.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRF--VDKEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYI 1325
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFdaDTKEWKERGVGEMKILYHPElNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1326 WVANDFA-DEELRLEKLCIKFKTVEEAASFKENFEKA 1361
Cdd:cd13174     81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
2516-2714 5.23e-31

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 122.82  E-value: 5.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2516 EQKPAFKTDPNFTfegaGASVFGVKNAQKTGDKTKKTPNSKKDKAKDDDDEDGDDEnengdehDPYFEPIIPLpDAIEVR 2595
Cdd:COG5171     16 ENEQKERSLDVVS----KGDAFGDGKAGGEEKKVQQSPFLENAVPEGDEGKGPESP-------NIHFEPVVEL-QRVHLK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWM 2675
Cdd:COG5171     84 TNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWV 163

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1227107233 2676 WA-GMNYAEADsPEVEQLAVRFKTPELASQFKEAVDKAQQ 2714
Cdd:COG5171    164 WMsTADTVEGE-AKAQTFAIRFYSEENAKRFKEEFEKGQE 202
RanBD5_RanBP2_insect-like cd13175
Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ...
 2764-2867 1.18e-30

Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 5 is present in this hierarchy.


Pssm-ID: 269996  Cd Length: 114  Bit Score: 118.02  E-value: 1.18e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNNE-LASETVISVDTTMQYNEKECTWAAIDYAVEPQ 2842
Cdd:cd13175      9 MFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDtIIANTIIAVQTSLRVEGKEAIWSAIDYSQEPL 88

                           90       100
                   ....*....|....*....|....*
gi 1227107233 2843 VRRTLRAVFSSSQTAEQMYQTFQEG 2867
Cdd:cd13175     89 LRRRFRAEFSSDDAAQEFSVVFNEG 113
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1203-1377 1.50e-29

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 118.58  E-value: 1.50e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1203 KPQDNQNSSLLSTGSRHSSSDVTEVEHDPIpDFAPIIPLpDEVPVTTGEENEEELYCARAKLFRFVD--KEWKERGIGNV 1280
Cdd:COG5171     40 GEEKKVQQSPFLENAVPEGDEGKGPESPNI-HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEeaKEWKERGTGDM 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1281 KLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIW-VANDFADEELRLEKLCIKFKTVEEAASFKENF 1358
Cdd:COG5171    118 IILKHKKtNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWmSTADTVEGEAKAQTFAIRFYSEENAKRFKEEF 197

                          170
                   ....*....|....*....
gi 1227107233 1359 EKAKdslpdEEAKPATETK 1377
Cdd:COG5171    198 EKGQ-----EHNEKALKTK 211
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1944-2055 5.11e-21

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 90.35  E-value: 5.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSAtKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWMWT 2023
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVG 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233 2024 AGDYSEGEIEYMqfaCRFKTPEIAADFKNAVD 2055
Cdd:cd13170     80 CVPNPGKPVTYL---LRVKTAEDADELAKALE 108
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1249-1362 4.21e-19

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 84.96  E-value: 4.21e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVD-KEWKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIW 1326
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDdGEWKDKGVGTLRLKKHKTtGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVGC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1227107233 1327 VANDFAdeelrLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13170     81 VPNPGK-----PVTYLLRVKTAEDADELAKALEEEK 111
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1944-2055 4.26e-17

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270002  Cd Length: 115  Bit Score: 79.40  E-value: 4.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKE--WKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWM 2021
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 2022 WTAGDYSEGEIEymQFACRFKTPeiaADFKNAVD 2055
Cdd:cd13181     81 RVPTINSDGKIE--TYVIKVKTA---ADGEELLK 109
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1944-2055 7.91e-17

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 78.43  E-value: 7.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDSATKEWKERGLGDIKLLRHVETKKL--RLVMRRDQVLKLCLNHAVTPALEISSKDDKTWM 2021
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGqsRIVMRTQGSLRVILNTKIWPGMTVEKVSEKSLR 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 2022 WTAGDyseGEIEYMQFACRFKtPEIAADFKNAVD 2055
Cdd:cd13180     81 ITAMD---DEGQVKVFLLQAS-PEDAKQLYNAIQ 110
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1249-1364 8.32e-17

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy.


Pssm-ID: 269990  Cd Length: 117  Bit Score: 78.65  E-value: 8.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRFVDKEWKERGIGNVKL-LKNTEGKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKAYIWV 1327
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFIDGGWKERGKGELRVnLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFACV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 1328 aNDFADEELRLEKLCIKFKTVEEAASFKENFEKAKDS 1364
Cdd:cd13169     81 -NSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHKDS 116
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1249-1362 2.42e-15

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270002  Cd Length: 115  Bit Score: 74.40  E-value: 2.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1249 TGEENEEELYCARAKLFRF--VDKE--WKERGIGNVKLLKNTE-GKIRLLMRREQVLKICANHMLRKDMELTMMKNNEKA 1323
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFdpSNTEspYTSKGVGELKLLKNKDtGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1227107233 1324 YIWVANdfadEELRLEKLCIKFKTVEEAASFKENFEKAK 1362
Cdd:cd13181     81 RVPTIN----SDGKIETYVIKVKTAADGEELLKALNDAK 115
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 2596-2713 5.32e-15

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 73.41  E-value: 5.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNtKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDrawM 2675
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---V 76

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233 2676 WAGMnyaEADSPEVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13170     77 FVGC---VPNPGKPVTYLLRVKTAEDADELAKALEEEK 111
Ran_BP1 pfam00638
RanBP1 domain;
1509-1616 1.01e-14

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 72.85  E-value: 1.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYN-QIVPPRTVFNLKSDTV 1587
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANhYITPDMTLKPLAGSDR 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 1588 NWT-----IENEKNKPDSYLARFKNYDQASLFQK 1616
Cdd:pfam00638   81 SWVwtaadFADGEGKPEQLAIRFKTKEEADSFKK 114
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1514-1618 2.71e-14

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 71.47  E-value: 2.71e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPR---TVFNLKSDTVNWT 1590
Cdd:cd00835      3 EENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDmklTKMGNNDRAWVWT 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233 1591 I----ENEKNKPDSYLARFKNYDQASLFQKSL 1618
Cdd:cd00835     83 AmddsEDGEGKPETFAVRFKTAEDAEEFKKAF 114
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1944-2054 4.04e-14

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy.


Pssm-ID: 269990  Cd Length: 117  Bit Score: 70.94  E-value: 4.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1944 TGEENEDVLYSHRAKLFKFDsaTKEWKERGLGDIKLLRHVETKKLRLVMRRDQVLKLCLNHAVTPALEISSKDDKTWMWT 2023
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFI--DGGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233 2024 AGDYSEGEIEYMQ-FACRFKTPEIAADFKNAV 2054
Cdd:cd13169     79 CVNSAADAKDKLStFALKFKDPQVVEEFRAAV 110
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 2596-2712 2.13e-13

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 68.80  E-value: 2.13e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKEWKERGTGEMKLLHHAEHGT--YRLLLRREQVHKVVcnllltsdlefreLNSSdra 2673
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSgqSRIVMRTQGSLRVI-------------LNTK--- 64

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2674 wMWAGMNYAEADSP-----------EVEQLAVRFKtPELASQFKEAVDKA 2712
Cdd:cd13180     65 -IWPGMTVEKVSEKslritamddegQVKVFLLQAS-PEDAKQLYNAIQDR 112
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 2596-2712 7.81e-13

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP#importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The first RanBD2 is present in this hierarchy.


Pssm-ID: 269990  Cd Length: 117  Bit Score: 67.47  E-value: 7.81e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNntKEWKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSsdRAWM 2675
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGG--KGVT 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1227107233 2676 WAGMNYAEADSPEVEQLAVRFKTPELASQFKEAVDKA 2712
Cdd:cd13169     77 FACVNSAADAKDKLSTFALKFKDPQVVEEFRAAVEAH 113
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 2596-2713 5.25e-12

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270002  Cd Length: 115  Bit Score: 64.77  E-value: 5.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2596 TGEEDEEKVFCHRAKLYRYDNNTKE--WKERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRA 2673
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1227107233 2674 wMWAGMNYAEAdspeVEQLAVRFKTPELASQFKEAVDKAQ 2713
Cdd:cd13181     81 -RVPTINSDGK----IETYVIKVKTAADGEELLKALNDAK 115
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 2763-2868 7.12e-12

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBP2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The RanBD proteins of the nuclear pore complex (NPC): nucleoporin 1 (NUP1), NUP2, NUP61, and Nuclear Pore complex Protein 9 (npp-9) are present in the parent, but specific models were not made due to lineage. To date there been no reports of inositol phosphate or phosphoinositide binding by Ran-binding proteins.


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 64.54  E-value: 7.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2763 TMFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVEND-------NNELASETVIsvdTTMQYNEKECTWAAI 2835
Cdd:cd00835      8 VLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDqvlklccNHYILPDMKL---TKMGNNDRAWVWTAM 84

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1227107233 2836 DYAV-EPQVRRTLRAVFSSSQTAEQMYQTFQEGL 2868
Cdd:cd00835     85 DDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1249-1312 7.99e-12

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 64.17  E-value: 7.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1227107233 1249 TGEENEEELYCARAKLFRFVD--KEWKERGIGNVKLLKNTE---GKIRLLMRREQVLKICANHMLRKDM 1312
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKskQSWKERGRGTLRLNDSKSdgsGQSRIVMRTQGSLRVILNTKIWPGM 69
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1505-1616 2.48e-11

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of Ran (the Ras-like nuclear small GTPase).


Pssm-ID: 197549  Cd Length: 130  Bit Score: 63.56  E-value: 2.48e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  1505 SKGSEVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEK-STGRVRLLMNTEDNSKTIYN-QIVPPRTVFNL 1582
Cdd:smart00160    7 LPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANhPIFKSMTLKPL 86

                            90       100       110
                    ....*....|....*....|....*....|....*....
gi 1227107233  1583 KSDTVNWTIENEKN-----KPDSYLARFKNYDQASLFQK 1616
Cdd:smart00160   87 AGSNRALKWTPEDFaddipKLVLYAVRFKTKEEADSFKN 125
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1618 6.14e-11

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269993  Cd Length: 118  Bit Score: 62.08  E-value: 6.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEK-STGRVRLLMNTEDNSKTIYNQIVPPRTVFNL--KSD-TVNW 1589
Cdd:cd13172      3 EENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKeDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYltNNPkALTW 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1227107233 1590 T----IENEKnKPDSYLARFKNYDQASLFQKSL 1618
Cdd:cd13172     83 CaqdySEGEL-KPETFAIRFKTQEICKDFLDAV 114
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1514-1616 1.21e-10

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 61.14  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPrtVFNLKSDTVN----- 1588
Cdd:cd13176      3 EEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITP--DMKLKPNAGSdrswv 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1227107233 1589 WT---IENEKNKPDSYLARFKNYDQASLFQK 1616
Cdd:cd13176     81 WTaldFSEEEPKVEQLAVKFKTPEVADEFKK 111
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1527-1615 3.13e-10

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 60.04  E-value: 3.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1527 LMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVF--NLKSD-TVNWT---IENEKNKPDS 1600
Cdd:cd14684     16 LFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLkpNAGSDkSFVWNaldYADELPKPEQ 95

                           90
                   ....*....|....*
gi 1227107233 1601 YLARFKNYDQASLFQ 1615
Cdd:cd14684     96 LAIRFKTVEEAALFK 110
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1509-1616 3.48e-09

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270000 [Multi-domain]  Cd Length: 136  Bit Score: 57.58  E-value: 3.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDN--KLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVF--NLKS 1584
Cdd:cd13179     14 EVKTGEEDEEVLFKMRAKLYRFDTENdpPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYITPEMKLkpNAGS 93

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1227107233 1585 D-TVNWTIEN---EKNKPDSYLARFKNYDQASLFQK 1616
Cdd:cd13179     94 DrAWVWTCADfadEEPKPELFAIRFANAENAQKFKE 129
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 2367-2467 7.28e-09

Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.


Pssm-ID: 463941 [Multi-domain]  Cd Length: 90  Bit Score: 54.93  E-value: 7.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2367 SIFG-TTTTITSLFGGTASTLPS----FGALANQGNTTANGGLFSSNTFGSTTPALDAKSTTVSAPASttttttvGSTIF 2441
Cdd:pfam13634    1 GLFGaATSTSGGLFGNTSTTAASggglFGAASTATATTSGGGLFGNSSSNAPSGGLFGATNTTTQTAT-------GGGLF 73

                           90       100
                   ....*....|....*....|....*.
gi 1227107233 2442 GGNAATQFTskltfgtgvAPTTNVFG 2467
Cdd:pfam13634   74 GNNAATTTS---------TTGGGLFG 90
Nucleoporin_FG pfam13634
Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in ...
 2333-2416 1.21e-08

Nucleoporin FG repeat region; This family includes a number of FG repeats that are found in nucleoporin proteins. This family includes the yeast nucleoporins Nup116, Nup100, Nup49, Nup57 and Nup 145.


Pssm-ID: 463941 [Multi-domain]  Cd Length: 90  Bit Score: 54.54  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2333 GIFGESKPPTANIFGGtaappaavtTTTTSSTTNSIFG------TTTTITSLFGGTASTLPS---FGALANQGNTTANGG 2403
Cdd:pfam13634    1 GLFGAATSTSGGLFGN---------TSTTAASGGGLFGaastatATTSGGGLFGNSSSNAPSgglFGATNTTTQTATGGG 71

                           90
                   ....*....|...
gi 1227107233 2404 LFSSNTFGSTTPA 2416
Cdd:pfam13634   72 LFGNNAATTTSTT 84
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1614 1.22e-08

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 269992  Cd Length: 117  Bit Score: 55.17  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSdnKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPR---TVFNLKSDTVNWT 1590
Cdd:cd13171      3 EENEEVLFCARAKLFRYVD--KEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDmelTPMKKEDKAYIWA 80

                           90       100
                   ....*....|....*....|....*..
gi 1227107233 1591 ---IENEKNKPDSYLARFKNYDQASLF 1614
Cdd:cd13171     81 andFADEVVVLEKLCVRFKTVELAKEF 107
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1616 2.25e-08

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269999  Cd Length: 117  Bit Score: 54.58  E-value: 2.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNiNLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPR---TVFNLKSDTVNWT 1590
Cdd:cd13178      4 EDEEILFKERA-KLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDmdlQPLSASNNTLVWT 82

                           90       100
                   ....*....|....*....|....*....
gi 1227107233 1591 IENEKN---KPDSYLARFKNYDQASLFQK 1616
Cdd:cd13178     83 ATDYADgegKVEQLAVRFKTKEIADSFKK 111
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1615 2.44e-08

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 2 is present in this hierarchy.


Pssm-ID: 269998 [Multi-domain]  Cd Length: 117  Bit Score: 54.67  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPprTVFNLK----SDTVNW 1589
Cdd:cd13177      3 EEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWIT--TTMNLKplagSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1227107233 1590 TIENEKNKPDSYL----ARFKNYDQASLFQ 1615
Cdd:cd13177     81 WMANDFSDGDAKLeqlaAKFKTPELAEEFK 110
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1618 2.97e-08

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 3 is present in this hierarchy.


Pssm-ID: 269994  Cd Length: 115  Bit Score: 54.03  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLmhYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVFNLKSDTV-NWTI- 1591
Cdd:cd13173      3 EEDEEVLYSHRAKL--FRFVDKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKDEKSwMWAAh 80

                           90       100       110
                   ....*....|....*....|....*....|
gi 1227107233 1592 ---ENEKnKPDSYLARFKNYDQASLFQKSL 1618
Cdd:cd13173     81 dfsEGES-ELERFAIRFKNAEIAQGFMKAI 109
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-140 7.44e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 53.66  E-value: 7.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLAdpEV 108
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALElDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALL--KA 85

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233  109 GiDVNRAKYWVDRADKLFPPHKSVFQLKEKIL 140
Cdd:COG4783     86 G-DYDEALALLEKALKLDPEHPEAYLRLARAY 116
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 14-215 2.20e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 55.12  E-value: 2.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   14 DIFRKLQDETERTLRCY-KIAELYYNVGDYESARRYLSRYVEF-RTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPR 91
Cdd:COG2956     29 DLLEEALELDPETVEAHlALGNLYRRRGEYDRAIRIHQKLLERdPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPD 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   92 QEELILKVCELLADPEvgiDVNRAKYWVDRADKLFPPHKSV-FQLKEKILSIERPTNNQEDLENLitaeLATRPTDVHLR 170
Cdd:COG2956    109 DAEALRLLAEIYEQEG---DWEKAIEVLERLLKLGPENAHAyCELAELYLEQGDYDEAIEALEKA----LKLDPDCARAL 181

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1227107233  171 VKLIKHYMERSKLDEAYKHATDIEAssIHRDSVIWYQVLCELFLK 215
Cdd:COG2956    182 LLLAELYLEQGDYEEAIAALERALE--QDPDYLPALPRLAELYEK 224
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 14-156 2.79e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 54.74  E-value: 2.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   14 DIFRKLQDETERTLRCY-KIAELYYNVGDYESARRYLSRYVEF-RTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPR 91
Cdd:COG2956    131 EVLERLLKLGPENAHAYcELAELYLEQGDYDEAIEALEKALKLdPDCARALLLLAELYLEQGDYEEAIAALERALEQDPD 210

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1227107233   92 QEELILKVCELLADPEvgiDVNRAKYWVDRADKLFPPHKSVFQLKEKILSIERPTNNQEDLENLI 156
Cdd:COG2956    211 YLPALPRLAELYEKLG---DPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQL 272
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1616 4.07e-07

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 50.87  E-value: 4.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNInLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVF---NLKSDTVNWT 1590
Cdd:cd13174      4 EDETKLFGERAK-LYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLrpmNTSDKSFTWG 82

                           90       100       110
                   ....*....|....*....|....*....|
gi 1227107233 1591 IEN--EKNKP--DSYLARFKNYDQASLFQK 1616
Cdd:cd13174     83 GMNyaEDAEPevETLAVRFKNEEIASQFKN 112
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1514-1606 5.91e-07

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270002  Cd Length: 115  Bit Score: 50.51  E-value: 5.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNK--LWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVFNL--KSDTVNW 1589
Cdd:cd13181      3 EENEEVLYTKRAKLMLFDPSNTesPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKmgNGSLVRV 82

                           90
                   ....*....|....*..
gi 1227107233 1590 TIENEKNKPDSYLARFK 1606
Cdd:cd13181     83 PTINSDGKIETYVIKVK 99
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 2-217 7.68e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 53.58  E-value: 7.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233    2 LRTKKEVDRHVQdIFRKLQDETERTLR-CYKIAELYYNVGDYESARRYLSRYVEFRTE-PKGHKLMGQILEALGQKEAAV 79
Cdd:COG2956     52 YRRRGEYDRAIR-IHQKLLERDPDRAEaLLELAQDYLKAGLLDRAEELLEKLLELDPDdAEALRLLAEIYEQEGDWEKAI 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   80 VQYKRAFELEPRQEELILKVCELLADPEvgiDVNRAKYWVDRADKLFPPHKSVFQLKEKILSIErptNNQEDLENLITAE 159
Cdd:COG2956    131 EVLERLLKLGPENAHAYCELAELYLEQG---DYDEAIEALEKALKLDPDCARALLLLAELYLEQ---GDYEEAIAALERA 204

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1227107233  160 LATRPTDVHLRVKLIKHYMERSKLDEAYKHAtdIEASSIHRDSVIWYqVLCELFLKCK 217
Cdd:COG2956    205 LEQDPDYLPALPRLAELYEKLGDPEEALELL--RKALELDPSDDLLL-ALADLLERKE 259
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-92 1.89e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 49.81  E-value: 1.89e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFRTE-PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQ 92
Cdd:COG4783     76 LNLGLALLKAGDYDEALALLEKALKLDPEhPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1530-1621 2.27e-06

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 269991  Cd Length: 111  Bit Score: 48.75  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1530 YTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVFNLKSDTVNWTI-ENEKNKPDSYLARFKNY 1608
Cdd:cd13170     18 KKKDDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVGcVPNPGKPVTYLLRVKTA 97

                           90
                   ....*....|...
gi 1227107233 1609 DQASLFQKSLMGY 1621
Cdd:cd13170     98 EDADELAKALEEE 110
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1655-1679 2.33e-06

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 46.16  E-value: 2.33e-06
                            10        20
                    ....*....|....*....|....*
gi 1227107233  1655 GSWECKGCYMRNSASAKSCVACQAP 1679
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 17-127 3.61e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 49.19  E-value: 3.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   17 RKLQDETERTLRCYKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEEL 95
Cdd:COG5010     45 AGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQlDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNA 124

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1227107233   96 ILKVCELLADPEvgiDVNRAKYWVDRADKLFP 127
Cdd:COG5010    125 YSNLAALLLSLG---QDDEAKAALQRALGTSP 153
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1514-1616 7.01e-06

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy.


Pssm-ID: 270204  Cd Length: 117  Bit Score: 47.65  E-value: 7.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQ-IVPPRTVFNLKSDTVNWT-- 1590
Cdd:cd14685      3 EENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHrITADMKLQPMKGSERAWVwt 82

                           90       100
                   ....*....|....*....|....*....
gi 1227107233 1591 ---IENEKNKPDSYLARFKNYDQASLFQK 1616
Cdd:cd14685     83 amdFAEGEGKIEQLAVRFKLQETADTFKQ 111
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1654-1682 7.67e-06

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 44.65  E-value: 7.67e-06
                           10        20
                   ....*....|....*....|....*....
gi 1227107233 1654 AGSWECKGCYMRNSASAKSCVACQAPSPS 1682
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPKPD 30
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1509-1627 1.17e-05

Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];


Pssm-ID: 227499  Cd Length: 211  Bit Score: 48.86  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1509 EVSRIEDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKVLFEKSTGRVRLLMNTEDNSKTIYNQIVPPRTVF--NLKSDT 1586
Cdd:COG5171     81 HLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLqpNVGSDR 160

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1227107233 1587 vNW-------TIENEKnKPDSYLARFKNYDQASLFQKSLMGYLEKSAK 1627
Cdd:COG5171    161 -SWvwmstadTVEGEA-KAQTFAIRFYSEENAKRFKEEFEKGQEHNEK 206
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 30-94 1.68e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 46.14  E-value: 1.68e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEfrTEPKGHK------LMGQILEALGQKEAAVVQYKRAFELEPRQEE 94
Cdd:COG1729     34 YWLGEAYYALGDYDEAAEAFEKLLK--RYPDSPKapdallKLGLSYLELGDYDKARATLEELIKKYPDSEA 102
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 30-215 1.85e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.96  E-value: 1.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFRTE-PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLADpeV 108
Cdd:COG2956     12 YFKGLNYLLNGQPDKAIDLLEEALELDPEtVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLK--A 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  109 GiDVNRAKYWVDRADKLFPPHKSVFQLKEKILSIERptnnqeDLENLI-TAE--LATRPTDVHLRVKLIKHYMERSKLDE 185
Cdd:COG2956     90 G-LLDRAEELLEKLLELDPDDAEALRLLAEIYEQEG------DWEKAIeVLErlLKLGPENAHAYCELAELYLEQGDYDE 162

                          170       180       190
                   ....*....|....*....|....*....|
gi 1227107233  186 AYKHATdiEASSIHRDSVIWYQVLCELFLK 215
Cdd:COG2956    163 AIEALE--KALKLDPDCARALLLLAELYLE 190
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
35-127 4.40e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 44.39  E-value: 4.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   35 LYYNVGDYESARRYLSRYVEFR-TEPKGHKLMGQILEALGQKEAAvVQYKRAFELEPRQEELILKVCELLAdpEVGiDVN 113
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDpDNADALNNLGLLLLEQGRYDEA-IALEKALKLDPNNAEALLNLAELLL--ELG-DYD 76

                           90
                   ....*....|....
gi 1227107233  114 RAKYWVDRADKLFP 127
Cdd:COG3063     77 EALAYLERALELDP 90
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
30-221 5.39e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.31  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFRTE-PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLAdpEV 108
Cdd:COG0457     46 YNLGLAYLRLGRYEEALADYEQALELDPDdAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALL--EL 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  109 GiDVNRAKYWVDRADKLFPPHKSVFQLKEKIL-SIERPTNNQEDLENLITAELATRPTDVHLRVKLIKHYMERSKLDEAY 187
Cdd:COG0457    124 G-RYDEAIEAYERALELDPDDADALYNLGIALeKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLA 202

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1227107233  188 KHATDIEASSIHRDSVIWYQVLCELFLKCKYNHQ 221
Cdd:COG0457    203 LEQALRKKLAILTLAALAELLLLALALLLALRLA 236
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
30-94 5.58e-05

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 47.31  E-value: 5.58e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEE 94
Cdd:COG0457     12 NNLGLAYRRLGRYEEAIEDYEKALElDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAE 77
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1711-1739 8.40e-05

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 41.57  E-value: 8.40e-05
                           10        20
                   ....*....|....*....|....*....
gi 1227107233 1711 AGSWECKDCYTRNDAGVTKCVACQAAAPG 1739
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPKPD 30
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1514-1616 1.06e-04

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.


Pssm-ID: 270001  Cd Length: 113  Bit Score: 43.76  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 1514 EDGEIVIAEQNINLMHYTSDNKLWKEKGIGIIKV--LFEKSTGRVRLLMNTEDNSKTIYN-QIVPPRTVFNLKSDTVNWT 1590
Cdd:cd13180      3 EEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNtKIWPGMTVEKVSEKSLRIT 82

                           90       100
                   ....*....|....*....|....*..
gi 1227107233 1591 -IENEKNkPDSYLARFKNYDQASLFQK 1616
Cdd:cd13180     83 aMDDEGQ-VKVFLLQASPEDAKQLYNA 108
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 59-307 1.29e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 47.77  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   59 PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQeeliLKVCELLADpeVGIDVNRAKYWVDRADKLFPPHKSVFQLKEK 138
Cdd:TIGR02917  465 ASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDF----FPAAANLAR--IDIQEGNPDDAIQRFEKVLTIDPKNLRAILA 538

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  139 ILSIERPTNNQEDLENLITAELATRPTDVHLRVKLIKHYMERSKLDEAYkhATDIEASSIHRDSVIWYQVLCELFLKCKy 218
Cdd:TIGR02917  539 LAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKAL--AILNEAADAAPDSPEAWLMLGRAQLAAG- 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233  219 NHQtmwsfwiSYISALERYAALsLKEQGSSVRKTSEAIQAVYNFDQHLFEAKgQSFSSYPSLTESIFVhmwgqlhfhLAC 298
Cdd:TIGR02917  616 DLN-------KAVSSFKKLLAL-QPDSALALLLLADAYAVMKNYAKAITSLK-RALELKPDNTEAQIG---------LAQ 677


                   ....*....
gi 1227107233  299 LLIQNTQRE 307
Cdd:TIGR02917  678 LLLAAKRTE 686
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 35-90 1.34e-04

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 46.83  E-value: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1227107233   35 LYYNVGDYESARRYLSRYVEFRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEP 90
Cdd:COG3071    267 LCLRNQLWGKAREYLEAALALRPSAEAYAELARLLEQLGDPEEAAEHYRKALALAL 322
EVH1_family cd00837
EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; ...
 2608-2712 1.38e-04

EVH1 (Drosophila Enabled (Ena)/Vasodilator-stimulated phosphoprotein (VASP) homology 1) domain; The EVH1 domains are part of the PH domain superfamily. EVH1 subfamilies include Enables/VASP, Homer/Vesl, WASP, and Spred. Ligands are known for three of the EVH1 subfamilies, all of which bind proline-rich sequences: the Enabled/VASP family binds to FPPPP peptides, the Homer/Vesl family binds PPxxF peptides, and the WASP family binds LPPPEP peptides. EVH1 has a PH-like fold, despite having minimal sequence similarity to PH or PTB domains.


Pssm-ID: 269909  Cd Length: 103  Bit Score: 43.22  E-value: 1.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2608 RAKLYRYDNNTKEW---KERGTGEMKLLHHAEHGTYRLLLRREQVHKVVCNLLLTSDLEFRELNSSDRAWmwagmnyaeA 2684
Cdd:cd00837      6 RAHVMQIDDSNKNWvpaGGKGASRVSYFKDTTRNSFRIIGVDIKDKKVVINCTITKNLVYNKATQTFHQW---------A 76

                           90       100
                   ....*....|....*....|....*...
gi 1227107233 2685 DSPEVeqLAVRFKTPELASQFKEAVDKA 2712
Cdd:cd00837     77 DDRTV--FGLNFASEEDATKFAEAVQEA 102
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1712-1735 2.70e-04

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 40.38  E-value: 2.70e-04
                            10        20
                    ....*....|....*....|....
gi 1227107233  1712 GSWECKDCYTRNDAGVTKCVACQA 1735
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGA 24
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 32-92 3.05e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.80  E-value: 3.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227107233   32 IAELYYNVGDYESARRYLSRYVEFR-TEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQ 92
Cdd:COG5010     94 LALLYSRSGDKDEAKEYYEKALALSpDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPLK 155
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 30-105 3.77e-04

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 46.14  E-value: 3.77e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFRTE-PKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILKVCELLAD 105
Cdd:COG3914    116 FNLGNLLLALGRLEEALAALRRALALNPDfAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQD 192
IR1-M pfam12185
Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...
 2086-2133 4.94e-04

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00638, pfam00641, pfam00160. There are two conserved sequence motifs: TFFC and EDF. Nup358/RanBP2 is a nucleoporin involved in ubiquitination of many different protein targets from various cellular pathways. It complexes with Ubc9, SUMO-1 and RanGAP1 to perform this function. This is the ligase domain which binds to Ubc9.


Pssm-ID: 463488  Cd Length: 60  Bit Score: 40.53  E-value: 4.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1227107233 2086 DIEVVYEIKVTPEEKAAALKLKLPENFYsykyksdcpgCRGCKDSDES 2133
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFF----------CGYSSDTDDG 38
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 2764-2866 7.43e-04

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269999  Cd Length: 117  Bit Score: 41.86  E-value: 7.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNN-ELASETVISVD---TTMQYNEKECTWAAIDYAV 2839
Cdd:cd13178      9 LFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVlKVCANHVITQDmdlQPLSASNNTLVWTATDYAD 88

                           90       100
                   ....*....|....*....|....*..
gi 1227107233 2840 EPQVRRTLRAVFSSSQTAEQMYQTFQE 2866
Cdd:cd13178     89 GEGKVEQLAVRFKTKEIADSFKKVFEE 115
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
29-125 8.68e-04

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 43.72  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   29 CYKIAELYYNVGDYESARRYLSRYV----EFRTePKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEE-----LILKV 99
Cdd:COG4700    127 LLGLAQALFELGRYAEALETLEKLIaknpDFKS-SDAHLLYARALEALGDLEAAEAELEALARRYSGPEAryryaKFLAR 205

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1227107233  100 -------CELLAdpEVGIDVNRA--------KYWVDRADKL 125
Cdd:COG4700    206 qgrtaeaKELLE--EILDEAKHMpkhyrrlnREWIREAKKL 244
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 30-139 1.11e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.53  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFR-TEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEELILkvceLLA---- 104
Cdd:COG4235     21 LLLGRAYLRLGRYDEALAAYEKALRLDpDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALY----LLGlaaf 96

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1227107233  105 ---DPEVGIDvnrakYWvDRADKLFPPHKSVFQLKEKI 139
Cdd:COG4235     97 qqgDYAEAIA-----AW-QKLLALLPADAPARLLEASI 128
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 2367-2487 1.93e-03

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 43.99  E-value: 1.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2367 SIFGTTTTITSLFGGTASTLPSFGALANQGNTTANGGLFSSNTFGSTTPALDAKSTTVSApASTTTTTTVGSTIFGGNAA 2446
Cdd:COG3210    813 NVTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAA-TAASITVGSGGVATSTGTA 891

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1227107233 2447 TQFTSKLTFGTGVAPTTNVFGNLSSGTSNIFGGSKPSIGDS 2487
Cdd:COG3210    892 NAGTLTNLGTTTNAASGNGAVLATVTATGTGGGGLTGGNAA 932
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 2764-2866 2.09e-03

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 3 is present in this hierarchy.


Pssm-ID: 270204  Cd Length: 117  Bit Score: 40.33  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNN-ELASETVISVDTTMQY---NEKECTWAAIDYAV 2839
Cdd:cd14685      9 VFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVlKLCANHRITADMKLQPmkgSERAWVWTAMDFAE 88

                           90       100
                   ....*....|....*....|....*..
gi 1227107233 2840 EPQVRRTLRAVFSSSQTAEQMYQTFQE 2866
Cdd:cd14685     89 GEGKIEQLAVRFKLQETADTFKQIFDE 115
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 2763-2866 2.36e-03

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeats 1 and 3 are present in this hierarchy.


Pssm-ID: 269997 [Multi-domain]  Cd Length: 117  Bit Score: 40.34  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2763 TMFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDN-NELASETVISVDTTMQYN---EKECTWAAIDYA 2838
Cdd:cd13176      8 VLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQvLKVCANHYITPDMKLKPNagsDRSWVWTALDFS 87

                           90       100
                   ....*....|....*....|....*...
gi 1227107233 2839 VEPQVRRTLRAVFSSSQTAEQMYQTFQE 2866
Cdd:cd13176     88 EEEPKVEQLAVKFKTPEVADEFKKKFEE 115
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
30-91 3.38e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.00  E-value: 3.38e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVEFRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPR 91
Cdd:COG3063     30 NNLGLLLLEQGRYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPS 91
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 1768-1790 3.56e-03

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 36.91  E-value: 3.56e-03
                            10        20
                    ....*....|....*....|...
gi 1227107233  1768 GSWECKQCYVVNSQSNQYCAACD 1790
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 29-95 3.58e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.06  E-value: 3.58e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1227107233   29 CYKIAELYYNVGDYESARRYLSRYVEFR-TEPKGHKLMGQILEALGQKEAAVVQYKRAFELEPRQEEL 95
Cdd:COG3914    149 YLNLGEALRRLGRLEEAIAALRRALELDpDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADA 216
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
1767-1793 4.06e-03

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 36.95  E-value: 4.06e-03
                           10        20
                   ....*....|....*....|....*..
gi 1227107233 1767 AGSWECKQCYVVNSQSNQYCAACDKAK 1793
Cdd:pfam00641    2 EGDWDCSKCLVQNFATSTKCVACQAPK 28
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 33-90 4.50e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.


Pssm-ID: 467942 [Multi-domain]  Cd Length: 306  Bit Score: 41.85  E-value: 4.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1227107233   33 AELYYNVGDYESARRYLSRYVE-FRTEPKGHKLMGQILEALGQKEAAVVQYKRAFELEP 90
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALElEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 2764-2866 5.27e-03

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include human, chicken, frog, tunicates, sea urchins, ticks, sea anemones, and sponges. RanBD repeat 1 is present in this hierarchy.


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 39.24  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2764 MFEKRATVYAQNEGEVSWKHVAMGNLKVLYDSSFFGVKIVVENDNN-ELASETVISVDTTMQYN---EKECTWAAIDYAV 2839
Cdd:cd14684      9 MFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVlKICANHYISADMKLKPNagsDKSFVWNALDYAD 88

                           90       100
                   ....*....|....*....|....*..
gi 1227107233 2840 EPQVRRTLRAVFSSSQTAEQMYQTFQE 2866
Cdd:cd14684     89 ELPKPEQLAIRFKTVEEAALFKCKFEE 115
PRK12688 PRK12688
flagellin; Reviewed
 2370-2480 7.14e-03

flagellin; Reviewed


Pssm-ID: 171664 [Multi-domain]  Cd Length: 751  Bit Score: 41.79  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233 2370 GTTTTITS--LFGGTASTLPSFGALANQGNTTANGGLFSSNTFGSTTPALDAKSTtvsaPASTTTTTTVGSTIfggnaat 2447
Cdd:PRK12688   145 GGATAATGatTLGGTAGSLAGTGATAGDGTTALTGTITLIATNGTTATGLLGNAQ----PADGDTLTVNGKTI------- 213

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1227107233 2448 qftsklTFGTGVAPTT-------NVFGNL---SSGTSNIFGGS 2480
Cdd:PRK12688   214 ------TFRSGAAPAStavpsgsGVSGNLvtdGNGNSTVYLGS 250
TPR_16 pfam13432
Tetratricopeptide repeat; This family is found predominantly at the C-terminus of ...
 30-85 9.70e-03

Tetratricopeptide repeat; This family is found predominantly at the C-terminus of transglutaminase enzyme core regions.


Pssm-ID: 433202 [Multi-domain]  Cd Length: 68  Bit Score: 36.93  E-value: 9.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1227107233   30 YKIAELYYNVGDYESARRYLSRYVE-FRTEPKGHKLM---GQILEALGQKEAAVVQYKRA 85
Cdd:pfam13432    1 LALARAALRAGDYDDAAAALEAALArFPESPDAAAALlllGLAALRQGRLAEAAAAYRAA 60
 
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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