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Conserved domains on  [gi|1836166221|ref|NP_001369273|]
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RANBP2-like and GRIP domain-containing protein 1 isoform 1 [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 ...
 1341-1457 1.77e-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: 262.98  E-value: 1.77e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1044-1160 6.33e-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: 249.96  E-value: 6.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1634-1694 5.95e-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: 125.23  E-value: 5.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836166221 1634 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1694
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 32-221 1.93e-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: 72.45  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  112 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 191
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 1836166221  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1697-1740 5.32e-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: 64.68  E-value: 5.32e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1836166221 1697 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1740
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 ...
 1341-1457 1.77e-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: 262.98  E-value: 1.77e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1044-1160 6.33e-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: 249.96  E-value: 6.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1327-1456 6.23e-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: 213.40  E-value: 6.23e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  1327 FEPVVPLPDlVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1405
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1836166221  1406 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1456
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1338-1459 1.56e-63

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 211.90  E-value: 1.56e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1338 EVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1417
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1836166221 1418 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1459
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1041-1162 1.22e-61

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 206.51  E-value: 1.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1041 ELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDR 1120
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1836166221 1121 AWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQRL 1162
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1030-1159 3.14e-48

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


Pssm-ID: 197549  Cd Length: 130  Bit Score: 168.33  E-value: 3.14e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  1030 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG-KPRMLMRRDQVLKVCANHWITT 1108
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1836166221  1109 TMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEEC 1159
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
968-1160 4.93e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 156.72  E-value: 4.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  968 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQCGKMANKANTSGDFEK---DDDACKTEDSDDIHFEPVVQMpEKVELVT 1044
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1045 GEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWMW 1124
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1836166221 1125 L-ASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:COG5171    165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1300-1462 2.30e-38

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 143.24  E-value: 2.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1300 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN 1379
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1380 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1458
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 1836166221 1459 AQEK 1462
Cdd:COG5171    203 HNEK 206
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1634-1694 5.95e-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: 125.23  E-value: 5.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836166221 1634 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1694
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 32-221 1.93e-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: 72.45  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  112 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 191
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 1836166221  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1697-1740 5.32e-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: 64.68  E-value: 5.32e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1836166221 1697 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1740
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
1698-1743 3.79e-12

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


Pssm-ID: 197860  Cd Length: 46  Bit Score: 62.24  E-value: 3.79e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1836166221  1698 ANVEHLKNVLLQFIFLKPgSERESLLPVINTMLQLSPEEKGKLAAV 1743
Cdd:smart00755    2 ANFEYLKNVLLQFLTLRE-SERETLLPVISTVLQLSPEEMQKLLEV 46
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 59-90 2.82e-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: 2.82e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1836166221    59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDP 32
TPR_1 pfam00515
Tetratricopeptide repeat;
59-90 4.05e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.02  E-value: 4.05e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1836166221   59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNP 32
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 32-90 2.90e-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: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
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 ...
 1341-1457 1.77e-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: 262.98  E-value: 1.77e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1044-1160 6.33e-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: 249.96  E-value: 6.33e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1341-1457 2.60e-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: 233.71  E-value: 2.60e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1044-1160 9.36e-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: 223.69  E-value: 9.36e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1327-1456 6.23e-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: 213.40  E-value: 6.23e-64
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  1327 FEPVVPLPDlVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1405
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1836166221  1406 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1456
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1338-1459 1.56e-63

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 211.90  E-value: 1.56e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1338 EVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1417
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1836166221 1418 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1459
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1041-1162 1.22e-61

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 206.51  E-value: 1.22e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1041 ELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDR 1120
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1836166221 1121 AWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQRL 1162
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1027-1160 9.79e-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: 192.78  E-value: 9.79e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1027 DIHFEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEIS--QWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANH 1104
Cdd:cd13179      1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836166221 1105 WITTTMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13179     80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1326-1457 1.60e-56

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: 192.40  E-value: 1.60e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1326 YFEPVVPLPdLVEVSSGEENEQVVFSHRAELYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 1403
Cdd:cd13179      3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1836166221 1404 TPDMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13179     82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1341-1457 1.52e-53

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: 183.18  E-value: 1.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1421 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1044-1160 4.63e-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: 175.86  E-value: 4.63e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1124 WLASDFSD-GDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
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 ...
 1044-1160 1.08e-50

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: 174.77  E-value: 1.08e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
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 ...
 1341-1457 3.24e-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: 173.60  E-value: 3.24e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1044-1160 3.09e-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: 167.82  E-value: 3.09e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1030-1159 3.14e-48

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


Pssm-ID: 197549  Cd Length: 130  Bit Score: 168.33  E-value: 3.14e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  1030 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG-KPRMLMRRDQVLKVCANHWITT 1108
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1836166221  1109 TMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEEC 1159
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1044-1160 5.19e-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: 161.35  E-value: 5.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
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 ...
 1341-1457 6.80e-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: 155.59  E-value: 6.80e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
968-1160 4.93e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 156.72  E-value: 4.93e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  968 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQCGKMANKANTSGDFEK---DDDACKTEDSDDIHFEPVVQMpEKVELVT 1044
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1045 GEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWMW 1124
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1836166221 1125 L-ASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
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 ...
 1341-1457 7.11e-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: 152.60  E-value: 7.11e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1419
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1420 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1044-1160 9.56e-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: 149.14  E-value: 9.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKN-EVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAW 1122
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1123 MWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1341-1457 2.44e-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: 145.32  E-value: 2.44e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERVWV 1420
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1341-1457 3.06e-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: 145.17  E-value: 3.06e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1420
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1421 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
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 ...
 1044-1158 3.41e-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: 144.92  E-value: 3.41e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEisQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDK--EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1158
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 ...
 1341-1457 3.50e-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: 141.84  E-value: 3.50e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1419
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1420 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13171     78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1300-1462 2.30e-38

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 143.24  E-value: 2.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1300 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQN 1379
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1380 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1458
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 1836166221 1459 AQEK 1462
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 ...
 1044-1158 2.52e-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: 133.76  E-value: 2.52e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAeiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPlsGSDRAWM 1123
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1836166221 1124 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1158
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 ...
 1044-1160 1.34e-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: 131.76  E-value: 1.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836166221 1124 WLASDFS-DGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
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 ...
 1342-1456 2.56e-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: 127.91  E-value: 2.56e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1342 GEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVW 1421
Cdd:cd13174      2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1836166221 1422 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 1456
Cdd:cd13174     82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117
Rab_bind pfam16704
Rab binding domain; This coiled-coil domain, found in GRIP and coiled-coil domain-containing ...
 1634-1694 5.95e-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: 125.23  E-value: 5.95e-34
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836166221 1634 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1694
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 ...
 1341-1457 9.60e-17

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


Pssm-ID: 269990  Cd Length: 117  Bit Score: 77.87  E-value: 9.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNM--KGTERV 1418
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMggKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1836166221 1419 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13169     79 CVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1044-1160 1.93e-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: 76.87  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDrawm 1123
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1836166221 1124 wLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13170     76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1342-1457 5.91e-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: 72.64  E-value: 5.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1342 GEENEQVVFSHRAELYRYDKDvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMslqNMKGTERVWVW 1421
Cdd:cd13170      2 GEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGM---PYSVAGKNNVF 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1836166221 1422 TACDFADGerKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13170     78 VGCVPNPG--KPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1044-1116 1.23e-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: 1.23e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG--KPRMLMRRDQVLKVCANHWITTTMNLKPLS 1116
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGsgQSRIVMRTQGSLRVILNTKIWPGMTVEKVS 75
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1341-1452 1.46e-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: 1.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYDKDVGQWKERGIGDIKI--LQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERV 1418
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVE--KVSEKS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1836166221 1419 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKI 1452
Cdd:cd13180     79 LRITA---MDDEGQVKVFLLQASPEDAKQLYNAI 109
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 32-221 1.93e-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: 72.45  E-value: 1.93e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  112 RAKYWvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 191
Cdd:COG2956    163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 1836166221  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1044-1160 1.95e-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: 68.23  E-value: 1.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAEISQ--WKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPL-SGSDR 1120
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMgNGSLV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1836166221 1121 AWMWLasdfsDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1160
Cdd:cd13181     81 RVPTI-----NSDGKIETYVIKVKTAADGEELLKALNDAK 115
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1044-1158 3.19e-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: 3.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1044 TGEEGEKVLYSQGVKLFRFDAeiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1123
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1836166221 1124 WLASdFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1158
Cdd:cd13169     79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112
GRIP pfam01465
GRIP domain; The GRIP (golgin-97, RanBP2alpha,Imh1p and p230/golgin-245) domain is found in ...
 1697-1740 5.32e-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: 64.68  E-value: 5.32e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1836166221 1697 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1740
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44
Grip smart00755
golgin-97, RanBP2alpha,Imh1p and p230/golgin-245;
1698-1743 3.79e-12

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


Pssm-ID: 197860  Cd Length: 46  Bit Score: 62.24  E-value: 3.79e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1836166221  1698 ANVEHLKNVLLQFIFLKPgSERESLLPVINTMLQLSPEEKGKLAAV 1743
Cdd:smart00755    2 ANFEYLKNVLLQFLTLRE-SERETLLPVISTVLQLSPEEMQKLLEV 46
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1341-1457 3.35e-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: 62.07  E-value: 3.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1341 SGEENEQVVFSHRAELYRYD--KDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERV 1418
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1836166221 1419 WVWTacdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13181     81 RVPT----INSDGKIETYVIKVKTAADGEELLKALNDAK 115
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 28-260 7.84e-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: 64.75  E-value: 7.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   28 GFYF-AKLYYEAKEYDLAKKYvctYLSVQERDPR---AHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELL 103
Cdd:COG2956     10 GWYFkGLNYLLNGQPDKAIDL---LEEALELDPEtveAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  104 CKNDVTDgRAKYWVERAAKLFPGSPAIYklkEHLLDC---EGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRL 180
Cdd:COG2956     87 LKAGLLD-RAEELLEKLLELDPDDAEAL---RLLAEIyeqEGD--WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  181 KDAVARCHEA-------ERNIALRSSLEWNscvvqtLKEYLESLQCLEsdksDWRATNTDLLLAYANLMLLTLSTRDVQE 253
Cdd:COG2956    161 DEAIEALEKAlkldpdcARALLLLAELYLE------QGDYEEAIAALE----RALEQDPDYLPALPRLAELYEKLGDPEE 230


                   ....*..
gi 1836166221  254 SRELLES 260
Cdd:COG2956    231 ALELLRK 237
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 29-138 3.35e-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: 59.82  E-value: 3.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   29 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDV 108
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGD 87

                           90       100       110
                   ....*....|....*....|....*....|
gi 1836166221  109 TDGRAKYWvERAAKLFPGSPAIYKLKEHLL 138
Cdd:COG4783     88 YDEALALL-EKALKLDPEHPEAYLRLARAY 116
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
29-259 2.19e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 60.02  E-value: 2.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   29 FYFAKLYYEAKEYDLAKKYvctY---LSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK 105
Cdd:COG0457     12 NNLGLAYRRLGRYEEAIED---YekaLELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  106 -NDVTDGRAKYwvERAAKLFPGSPAIYKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAV 184
Cdd:COG0457     89 lGRYEEALEDY--DKALELDPDDAEALYNLGLALLELGR--YDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEAL 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1836166221  185 ARCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLE 259
Cdd:COG0457    165 ELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 58-131 1.30e-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: 1.30e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836166221   58 DPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFPGSPAIY 131
Cdd:COG4235     16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE-EAEELLERALALDPDNPEAL 88
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 6-125 3.48e-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: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221    6 AYGERYVASVQGSAPSPGKKLRGFYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRS 85
Cdd:COG5010     35 NNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKA 114

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1836166221   86 LELNPPQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFP 125
Cdd:COG5010    115 LALSPDNPNAYSNLAALLLSLGQDD-EAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-298 3.98e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.09  E-value: 3.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   52 LSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-NDVTDGRAKYwvERAAKLFPGSPAI 130
Cdd:COG0457      1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRlGRYEEALADY--EQALELDPDDAEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  131 YKLKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEA-ERNIALRSSLEWNSCVVQT 209
Cdd:COG0457     79 LNNLGLALQALGR--YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAlELDPDDADALYNLGIALEK 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  210 LKEYLESLQCLEsdkSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLESFDSALQSAKSSLGGNDELSATFLEMKGHF 289
Cdd:COG0457    157 LGRYEEALELLE---KLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233


                   ....*....
gi 1836166221  290 YMHAGSLLL 298
Cdd:COG0457    234 RLAALALYQ 242
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
32-193 1.54e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDG 111
Cdd:COG0457     83 GLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEE 162

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  112 RAKYWVERAAKLFPGSPAIYKLKEHLLDCEGEDGWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEAE 191
Cdd:COG0457    163 ALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQ 242


                   ..
gi 1836166221  192 RN 193
Cdd:COG0457    243 YR 244
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
34-125 2.32e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.47  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   34 LYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVEcYRRSLELNPPQKDLVLKIAELLCKNDVTDgRA 113
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD-EA 78

                           90
                   ....*....|..
gi 1836166221  114 KYWVERAAKLFP 125
Cdd:COG3063     79 LAYLERALELDP 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-125 2.64e-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: 48.65  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   30 YFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVT 109
Cdd:COG4783     43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                           90
                   ....*....|....*.
gi 1836166221  110 DGRAKYWvERAAKLFP 125
Cdd:COG4783    123 DEAIAAL-EKALELDP 137
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 29-97 6.70e-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: 6.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1836166221   29 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVL 97
Cdd:COG4235     55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARL 123
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 29-90 7.10e-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: 7.10e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1836166221   29 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:COG4783     76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 59-90 2.82e-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: 2.82e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 1836166221    59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDP 32
TPR_1 pfam00515
Tetratricopeptide repeat;
59-90 4.05e-05

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 42.02  E-value: 4.05e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1836166221   59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNP 32
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 31-131 5.66e-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: 5.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   31 FAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-NDVT 109
Cdd:COG3914     84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRlGRLE 163

                           90       100
                   ....*....|....*....|..
gi 1836166221  110 DGRAKYwvERAAKLFPGSPAIY 131
Cdd:COG3914    164 EAIAAL--RRALELDPDNAEAL 183
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 29-174 6.88e-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: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   29 FYFAKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCK-ND 107
Cdd:COG3914    116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDlGR 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221  108 VTDGRAKYwvERAAKLFPGSPAIYKLKEHLL----DCEGEDGWNKLFDWIQSE---------LYVRPDDVHMNIRLVELY 174
Cdd:COG3914    196 LEEAIAAY--RRALELDPDNADAHSNLLFALrqacDWEVYDRFEELLAALARGpselspfalLYLPDDDPAELLALARAW 273
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 32-88 1.31e-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: 1.31e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSvQERDPRAHRFLGLLYELEENTEKAVECYRRSLEL 88
Cdd:COG3071    265 GRLCLRNQLWGKAREYLEAALA-LRPSAEAYAELARLLEQLGDPEEAAEHYRKALAL 320
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
32-90 1.38e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 42.46  E-value: 1.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836166221   32 AKLYYEAKEYDLAKKYVcTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:COG3063     33 GLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 59-90 1.65e-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: 1.65e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1836166221   59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDP 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 56-190 4.59e-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: 42.10  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   56 ERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLckndVTDGR---AKYWVERAAKLFPGSPAIYK 132
Cdd:COG4783      1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEIL----LQLGDldeAIVLLHEALELDPDEPEARL 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836166221  133 LKEHLLDCEGEdgWNKLFDWIQSELYVRPDDVHMNIRLVELYRSNKRLKDAVARCHEA 190
Cdd:COG4783     77 NLGLALLKAGD--YDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKA 132
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 33-137 4.93e-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: 41.52  E-value: 4.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   33 KLYYEAKEYDLAKKYvctYLSVQERDP------RAHRFLGLLYELEENTEKAVECYRRSLELNPPQK---DLVLKIAELL 103
Cdd:COG1729      1 KALLKAGDYDEAIAA---FKAFLKRYPnsplapDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSY 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1836166221  104 CKNDVTDgRAKYWVERAAKLFPGSPAIYKLKEHL 137
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 ...
 1343-1457 7.88e-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: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221 1343 EENEQVVFSHRAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSlqnMKGTERVWVWT 1422
Cdd:cd13175      3 DDEELFMFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDTIIANTIIAVQTS---LRVEGKEAIWS 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1836166221 1423 ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1457
Cdd:cd13175     80 AIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK 114
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
34-90 1.82e-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: 1.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1836166221   34 LYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:COG4785     82 AYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDP 138
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
68-143 2.34e-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: 2.34e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1836166221   68 LYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDGRAKYwvERAAKLFPGSPAIYKLKEHLLDCEGE 143
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL--EKALKLDPNNAEALLNLAELLLELGD 74
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 32-90 2.90e-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: 2.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 32-131 2.95e-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: 2.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836166221   32 AKLYYEAKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDLVLKIAELLCKNDVTDg 111
Cdd:COG5010     27 YEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKD- 105

                           90       100
                   ....*....|....*....|
gi 1836166221  112 RAKYWVERAAKLFPGSPAIY 131
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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