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Conserved domains on  [gi|2462573210|ref|XP_054198003|]
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RANBP2-like and GRIP domain-containing protein 1 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.03e-81

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: 263.75  E-value: 1.03e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 3.20e-77

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: 250.73  E-value: 3.20e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
Apc1_MidN super family cl48671
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
 1-69 3.30e-41

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


The actual alignment was detected with superfamily member pfam20518:

Pssm-ID: 466667  Cd Length: 371  Bit Score: 156.80  E-value: 3.30e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210    1 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNVMGFNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 69
Cdd:pfam20518   23 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 91
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1707-1767 2.40e-34

Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing protein 2 and RANBP2-like and GRIP domain-containing protein, has been shown to bind to Rab in GRIP and coiled-coil domain-containing protein 2.


:

Pssm-ID: 435531  Cd Length: 65  Bit Score: 126.39  E-value: 2.40e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462573210 1707 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1767
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 105-294 1.37e-13

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: 73.22  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 184
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  185 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 264
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462573210  265 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 294
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1770-1813 4.40e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


:

Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 65.07  E-value: 4.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462573210 1770 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1813
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
 
Name Accession Description Interval E-value
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.03e-81

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: 263.75  E-value: 1.03e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 3.20e-77

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: 250.73  E-value: 3.20e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1400-1529 2.50e-64

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: 214.56  E-value: 2.50e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  1400 FEPVVPLPDlVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1478
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462573210  1479 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1529
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1411-1532 6.24e-64

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 213.06  E-value: 6.24e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1411 EVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1490
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462573210 1491 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1532
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1114-1235 5.08e-62

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 207.67  E-value: 5.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1114 ELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDR 1193
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462573210 1194 AWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQRL 1235
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1103-1232 1.60e-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: 169.11  E-value: 1.60e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  1103 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG-KPRMLMRRDQVLKVCANHWITT 1181
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462573210  1182 TMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEEC 1232
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1041-1233 1.55e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 158.26  E-value: 1.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1041 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQCGKMANKANTSGDFEK---DDDACKTEDSDDIHFEPVVQMpEKVELVT 1117
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1118 GEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWMW 1197
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462573210 1198 L-ASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:COG5171    165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201
Apc1_MidN pfam20518
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
 1-69 3.30e-41

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


Pssm-ID: 466667  Cd Length: 371  Bit Score: 156.80  E-value: 3.30e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210    1 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNVMGFNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 69
Cdd:pfam20518   23 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 91
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1373-1535 9.44e-39

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 144.39  E-value: 9.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1373 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN 1452
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1453 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1531
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 2462573210 1532 AQEK 1535
Cdd:COG5171    203 HNEK 206
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1707-1767 2.40e-34

Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing protein 2 and RANBP2-like and GRIP domain-containing protein, has been shown to bind to Rab in GRIP and coiled-coil domain-containing protein 2.


Pssm-ID: 435531  Cd Length: 65  Bit Score: 126.39  E-value: 2.40e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462573210 1707 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1767
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 105-294 1.37e-13

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: 73.22  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 184
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  185 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 264
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462573210  265 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 294
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1770-1813 4.40e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 65.07  E-value: 4.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462573210 1770 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1813
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
1771-1816 3.19e-12

golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;


Pssm-ID: 197860  Cd Length: 46  Bit Score: 62.62  E-value: 3.19e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2462573210  1771 ANVEHLKNVLLQFIFLKPgSERESLLPVINTMLQLSPEEKGKLAAV 1816
Cdd:smart00755    2 ANFEYLKNVLLQFLTLRE-SERETLLPVISTVLQLSPEEMQKLLEV 46
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 132-163 2.92e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 42.43  E-value: 2.92e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462573210   132 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDP 32
TPR_1 pfam00515
Tetratricopeptide repeat;
132-163 4.23e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.02  E-value: 4.23e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462573210  132 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNP 32
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 105-163 2.64e-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: 2.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
 
Name Accession Description Interval E-value
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.03e-81

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: 263.75  E-value: 1.03e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 3.20e-77

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: 250.73  E-value: 3.20e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1414-1530 1.79e-71

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: 234.48  E-value: 1.79e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1117-1233 6.51e-68

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: 224.08  E-value: 6.51e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1400-1529 2.50e-64

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: 214.56  E-value: 2.50e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  1400 FEPVVPLPDlVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1478
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462573210  1479 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1529
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1411-1532 6.24e-64

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 213.06  E-value: 6.24e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1411 EVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1490
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462573210 1491 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1532
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1114-1235 5.08e-62

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 207.67  E-value: 5.08e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1114 ELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDR 1193
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462573210 1194 AWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQRL 1235
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1100-1233 5.67e-57

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: 193.55  E-value: 5.67e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1100 DIHFEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEIS--QWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANH 1177
Cdd:cd13179      1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462573210 1178 WITTTMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13179     80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1399-1530 8.59e-57

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: 193.17  E-value: 8.59e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1399 YFEPVVPLPdLVEVSSGEENEQVVFSHRAELYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 1476
Cdd:cd13179      3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462573210 1477 TPDMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13179     82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1414-1530 9.97e-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: 183.57  E-value: 9.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1494 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1117-1233 3.01e-51

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: 176.63  E-value: 3.01e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1197 WLASDFSD-GDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD3_RanBP2-like cd14685
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 7.11e-51

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: 175.54  E-value: 7.11e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.91e-50

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: 174.37  E-value: 1.91e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1103-1232 1.60e-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: 169.11  E-value: 1.60e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  1103 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG-KPRMLMRRDQVLKVCANHWITT 1181
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462573210  1182 TMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEEC 1232
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 1.86e-48

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: 168.59  E-value: 1.86e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 2.81e-46

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: 162.12  E-value: 2.81e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117
RanBD2_RanBP2-like cd13177
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 4.42e-44

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: 155.98  E-value: 4.42e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1041-1233 1.55e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 158.26  E-value: 1.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1041 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQCGKMANKANTSGDFEK---DDDACKTEDSDDIHFEPVVQMpEKVELVT 1117
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1118 GEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWMW 1197
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462573210 1198 L-ASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:COG5171    165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 4.28e-43

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: 153.38  E-value: 4.28e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1492
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1493 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
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 ...
 1117-1233 5.70e-42

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: 149.91  E-value: 5.70e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKN-EVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAW 1195
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1196 MWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118
Apc1_MidN pfam20518
Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the ...
 1-69 3.30e-41

Anaphase-promoting complex subunit 1 middle domain; Apc1 is the largest of the subunits of the anaphase-promoting complex or cyclosome. The anaphase-promoting complex is a multiprotein subunit E3 ubiquitin ligase complex that controls segregation of chromosomes and exit from mitosis in eukaryotes. Apc1 consists of a N-terminal WD40 beta-propeller domain, followed by the middle domain (Mid-N), a PC domain and the C-terminal domain (MidC). This entry represents the middle domain of Apc1, MidN (also referred to as the first helical domain), that coaleses with the C-terminal domain to form Apc1Mid that connects Apc1WD40 with Apc1PC. Apc1Mid consists of an alpha-solenoid capped by a beta-sandwich.


Pssm-ID: 466667  Cd Length: 371  Bit Score: 156.80  E-value: 3.30e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210    1 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNVMGFNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 69
Cdd:pfam20518   23 MLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDD 91
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.66e-40

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: 145.70  E-value: 1.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERVWV 1493
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAK 113
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 1.74e-40

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: 145.94  E-value: 1.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1493
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1494 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1231 2.26e-40

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: 145.30  E-value: 2.26e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEisQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDK--EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1231
Cdd:cd13171     79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTK 113
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1414-1530 2.30e-39

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: 142.61  E-value: 2.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1492
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1493 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13171     78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1373-1535 9.44e-39

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 144.39  E-value: 9.44e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1373 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN 1452
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1453 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1531
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 2462573210 1532 AQEK 1535
Cdd:COG5171    203 HNEK 206
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1231 1.72e-36

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: 134.15  E-value: 1.72e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAeiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPlsGSDRAWM 1196
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462573210 1197 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1231
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1117-1233 1.12e-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 insects and nematodes. RanBD repeat 4 is present in this hierarchy.


Pssm-ID: 269995  Cd Length: 118  Bit Score: 132.15  E-value: 1.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462573210 1197 WLASDFS-DGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13174     81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1415-1529 2.14e-34

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: 128.29  E-value: 2.14e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1415 GEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVW 1494
Cdd:cd13174      2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462573210 1495 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 1529
Cdd:cd13174     82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1707-1767 2.40e-34

Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing protein 2 and RANBP2-like and GRIP domain-containing protein, has been shown to bind to Rab in GRIP and coiled-coil domain-containing protein 2.


Pssm-ID: 435531  Cd Length: 65  Bit Score: 126.39  E-value: 2.40e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462573210 1707 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1767
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1414-1530 1.00e-16

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: 77.87  E-value: 1.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNM--KGTERV 1491
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMggKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462573210 1492 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13169     79 CVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1117-1233 1.55e-16

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: 77.26  E-value: 1.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDrawm 1196
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462573210 1197 wLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13170     76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1415-1530 4.75e-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: 73.02  E-value: 4.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1415 GEENEQVVFSHRAELYRYDKDvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMslqNMKGTERVWVW 1494
Cdd:cd13170      2 GEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGM---PYSVAGKNNVF 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462573210 1495 TACDFADGerKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13170     78 VGCVPNPG--KPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1117-1189 1.16e-14

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: 71.88  E-value: 1.16e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG--KPRMLMRRDQVLKVCANHWITTTMNLKPLS 1189
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGsgQSRIVMRTQGSLRVILNTKIWPGMTVEKVS 75
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1414-1525 1.38e-14

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: 71.49  E-value: 1.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKI--LQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERV 1491
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVE--KVSEKS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462573210 1492 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKI 1525
Cdd:cd13180     79 LRITA---MDDEGQVKVFLLQASPEDAKQLYNAI 109
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1117-1233 1.33e-13

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: 69.00  E-value: 1.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAEISQ--WKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPL-SGSDR 1193
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMgNGSLV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462573210 1194 AWMWLasdfsDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1233
Cdd:cd13181     81 RVPTI-----NSDGKIETYVIKVKTAADGEELLKALNDAK 115
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 105-294 1.37e-13

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: 73.22  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 184
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  185 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 264
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462573210  265 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 294
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1117-1231 3.33e-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: 67.86  E-value: 3.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1117 TGEEGEKVLYSQGVKLFRFDAeiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1196
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462573210 1197 WLASdFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1231
Cdd:cd13169     79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1770-1813 4.40e-13

GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in many large coiled-coil proteins. It has been shown to be sufficient for targeting to the Golgi. The GRIP domain contains a completely conserved tyrosine residue. At least some of these domains have been shown to bind to GTPase Arl1, see structures in.


Pssm-ID: 460221 [Multi-domain]  Cd Length: 44  Bit Score: 65.07  E-value: 4.40e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2462573210 1770 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1813
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
1771-1816 3.19e-12

golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;


Pssm-ID: 197860  Cd Length: 46  Bit Score: 62.62  E-value: 3.19e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 2462573210  1771 ANVEHLKNVLLQFIFLKPgSERESLLPVINTMLQLSPEEKGKLAAV 1816
Cdd:smart00755    2 ANFEYLKNVLLQFLTLRE-SERETLLPVISTVLQLSPEEMQKLLEV 46
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1414-1530 2.57e-11

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: 62.45  E-value: 2.57e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1414 SGEENEQVVFSHRAELYRYD--KDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERV 1491
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462573210 1492 WVWTacdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13181     81 RVPT----INSDGKIETYVIKVKTAADGEELLKALNDAK 115
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 101-333 5.05e-11

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: 65.52  E-value: 5.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  101 GFYF-AKLYYEAKEYDLAKKYvctYLSVQERDP---RAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELL 176
Cdd:COG2956     10 GWYFkGLNYLLNGQPDKAIDL---LEEALELDPetvEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  177 CKNDVTDgRAKYWVERAAKLFPGSPAIYklkEHLLDC---EGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRL 253
Cdd:COG2956     87 LKAGLLD-RAEELLEKLLELDPDDAEAL---RLLAEIyeqEGD--WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  254 KDAVARCHEA-------ERNIALRSSLEWNscvvqtLKEYLESLQCLEsdksDWRATNTDLLLAYANLMLLTLSTRDVQE 326
Cdd:COG2956    161 DEAIEALEKAlkldpdcARALLLLAELYLE------QGDYEEAIAALE----RALEQDPDYLPALPRLAELYEKLGDPEE 230


                   ....*..
gi 2462573210  327 SRELLES 333
Cdd:COG2956    231 ALELLRK 237
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 102-211 2.70e-10

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: 60.21  E-value: 2.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  102 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDV 181
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGD 87

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462573210  182 TDGRAKYWvERAAKLFPGSPAIYKLKEHLL 211
Cdd:COG4783     88 YDEALALL-EKALKLDPEHPEAYLRLARAY 116
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
102-332 1.60e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.41  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  102 FYFAKLYYEAKEYDLAKKYvctY---LSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK 178
Cdd:COG0457     12 NNLGLAYRRLGRYEEAIED---YekaLELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  179 -NDVTDGRAKYwvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAV 257
Cdd:COG0457     89 lGRYEEALEDY--DKALELDPDDAEALYNLGLALLELGR--YDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEAL 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462573210  258 ARCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLE 332
Cdd:COG0457    165 ELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 131-204 1.28e-07

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: 52.32  E-value: 1.28e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462573210  131 DPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFPGSPAIY 204
Cdd:COG4235     16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE-EAEELLERALALDPDNPEAL 88
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
125-371 3.23e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.47  E-value: 3.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  125 LSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-NDVTDGRAKYwvERAAKLFPGSPAI 203
Cdd:COG0457      1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRlGRYEEALADY--EQALELDPDDAEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  204 YKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEA-ERNIALRSSLEWNSCVVQT 282
Cdd:COG0457     79 LNNLGLALQALGR--YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAlELDPDDADALYNLGIALEK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  283 LKEYLESLQCLEsdkSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLESFDSALQSAKSSLGGNDELSATFLEMKGHF 362
Cdd:COG0457    157 LGRYEEALELLE---KLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233


                   ....*....
gi 2462573210  363 YMHAGSLLL 371
Cdd:COG0457    234 RLAALALYQ 242
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 79-198 3.72e-07

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: 51.50  E-value: 3.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210   79 AYGERYVASVQGSAPSPGKKLRGFYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRS 158
Cdd:COG5010     35 NNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKA 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462573210  159 LELNPPQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFP 198
Cdd:COG5010    115 LALSPDNPNAYSNLAALLLSLGQDD-EAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
105-266 1.32e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 184
Cdd:COG0457     83 GLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  185 RAKYWVERAAKLFPGSPAIYKLKEHLLDCEGEDGWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 264
Cdd:COG0457    163 ALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQ 242


                   ..
gi 2462573210  265 RN 266
Cdd:COG0457    243 YR 244
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
107-198 1.90e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.86  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  107 LYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVEcYRRSLELNPPQKDLVLKIAELLCKNDVTDgRA 186
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD-EA 78

                           90
                   ....*....|..
gi 2462573210  187 KYWVERAAKLFP 198
Cdd:COG3063     79 LAYLERALELDP 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 103-198 2.11e-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: 49.03  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  103 YFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVT 182
Cdd:COG4783     43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                           90
                   ....*....|....*.
gi 2462573210  183 DGRAKYWvERAAKLFP 198
Cdd:COG4783    123 DEAIAAL-EKALELDP 137
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 102-163 6.07e-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: 47.49  E-value: 6.07e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462573210  102 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:COG4783     76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 102-170 6.55e-06

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: 47.31  E-value: 6.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210  102 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVL 170
Cdd:COG4235     55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 132-163 2.92e-05

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 42.43  E-value: 2.92e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 2462573210   132 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDP 32
TPR_1 pfam00515
Tetratricopeptide repeat;
132-163 4.23e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.02  E-value: 4.23e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462573210  132 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNP 32
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 104-204 5.94e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.07  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  104 FAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-NDVT 182
Cdd:COG3914     84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRlGRLE 163

                           90       100
                   ....*....|....*....|..
gi 2462573210  183 DGRAKYwvERAAKLFPGSPAIY 204
Cdd:COG3914    164 EAIAAL--RRALELDPDNAEAL 183
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 102-247 7.22e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.68  E-value: 7.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  102 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-ND 180
Cdd:COG3914    116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDlGR 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  181 VTDGRAKYwvERAAKLFPGSPAIYKLKEHLL----DCEGEDGWNKLFDWIQSE---------LYVRPDDVHMNIRLVELY 247
Cdd:COG3914    196 LEEAIAAY--RRALELDPDNADAHSNLLFALrqacDWEVYDRFEELLAALARGpselspfalLYLPDDDPAELLALARAW 273
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
105-163 1.20e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.85  E-value: 1.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210  105 AKLYYEAKEYDLAKKYVcTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:COG3063     33 GLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 105-161 1.28e-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: 46.06  E-value: 1.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSvQERDPRAHRFLGLLYELEENTEKAVECYRRSLEL 161
Cdd:COG3071    265 GRLCLRNQLWGKAREYLEAALA-LRPSAEAYAELARLLEQLGDPEEAAEHYRKALAL 320
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 132-163 1.72e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 40.20  E-value: 1.72e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462573210  132 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 129-263 3.75e-04

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: 42.49  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  129 ERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLckndVTDGR---AKYWVERAAKLFPGSPAIYK 205
Cdd:COG4783      1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIL----LQLGDldeAIVLLHEALELDPDEPEARL 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462573210  206 LKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEA 263
Cdd:COG4783     77 NLGLALLKAGD--YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKA 132
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 106-210 3.89e-04

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: 41.90  E-value: 3.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  106 KLYYEAKEYDLAKKYvctYLSVQERDP------RAHRFLGLLYELEENTEKAVECYRRSLELNPPQK---DLVLKIAELL 176
Cdd:COG1729      1 KALLKAGDYDEAIAA---FKAFLKRYPnsplapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSY 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462573210  177 CKNDVTDgRAKYWVERAAKLFPGSPAIYKLKEHL 210
Cdd:COG1729     78 LELGDYD-KARATLEELIKKYPDSEAAKEARARL 110
RanBD5_RanBP2_insect-like cd13175
Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ...
 1416-1530 8.24e-04

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: 40.98  E-value: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210 1416 EENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSlqnMKGTERVWVWT 1495
Cdd:cd13175      3 DDEELFMFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDTIIANTIIAVQTS---LRVEGKEAIWS 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462573210 1496 ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1530
Cdd:cd13175     80 AIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK 114
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
107-163 1.91e-03

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 41.82  E-value: 1.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462573210  107 LYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:COG4785     82 AYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDP 138
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
141-216 2.10e-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: 2.10e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462573210  141 LYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDGRAKYwvERAAKLFPGSPAIYKLKEHLLDCEGE 216
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL--EKALKLDPNNAEALLNLAELLLELGD 74
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 105-163 2.64e-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: 2.64e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 163
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 105-204 3.06e-03

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: 40.33  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462573210  105 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDg 184
Cdd:COG5010     27 YEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKD- 105

                           90       100
                   ....*....|....*....|
gi 2462573210  185 RAKYWVERAAKLFPGSPAIY 204
Cdd:COG5010    106 EAKEYYEKALALSPDNPNAY 125
 
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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