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Conserved domains on  [gi|767919496|ref|XP_011510035|]
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RANBP2-like and GRIP domain-containing protein 8 isoform X2 [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 ...
 1348-1464 3.71e-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: 261.82  E-value: 3.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
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 ...
 1051-1167 3.25e-78

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: 253.43  E-value: 3.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 33-222 2.09e-15

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: 78.23  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDG 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  113 RAKYWvERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 767919496  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
PRK08581 super family cl35718
amidase domain-containing protein;
1504-1680 1.39e-03

amidase domain-containing protein;


The actual alignment was detected with superfamily member PRK08581:

Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 43.24  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1504 TDVIQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFVSESVKRIFSS----EKSKPFAFGNSSATGSLfgfsfnAPLKS 1579
Cdd:PRK08581   55 TSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTninqLLTKNKYDDNYSLTTLI------QNLFN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1580 NNSETSSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLSAS----FPTEESSINYTFKTPEKGFNFSLFKSNPMAfw 1655
Cdd:PRK08581  129 LNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADnqkaPSSNNTKPSTSNKQPNSPKPTQPNQSNSQP-- 206

                         170       180
                  ....*....|....*....|....*
gi 767919496 1656 TSTPSSQPESKAKEKKKPEDSPSDS 1680
Cdd:PRK08581  207 ASDDTANQKSSSKDNQSMSDSALDS 231
 
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 ...
 1348-1464 3.71e-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: 261.82  E-value: 3.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
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 ...
 1051-1167 3.25e-78

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: 253.43  E-value: 3.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1334-1463 1.37e-63

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: 212.25  E-value: 1.37e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   1334 FEPVVPLPDlVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1412
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767919496   1413 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1463
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1345-1466 6.78e-63

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 209.98  E-value: 6.78e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  1345 EVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1424
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767919496  1425 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1466
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1048-1169 1.88e-62

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 208.44  E-value: 1.88e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  1048 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1127
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767919496  1128 AWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQRL 1169
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1037-1166 7.46e-49

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


Pssm-ID: 197549  Cd Length: 130  Bit Score: 169.88  E-value: 7.46e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   1037 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 1115
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767919496   1116 TMNLKPLSGSDRAWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEEC 1166
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
975-1167 4.16e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 156.72  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  975 AKSTSGEGFQ-------FGKKDLnfkgFSGAGEKLFSSRYGKMANKANTSGdfEKDDDayKTEDSDDIHFEPVVQMpEKV 1047
Cdd:COG5171    10 AKIEKEENEQkersldvVSKGDA----FGDGKAGGEEKKVQQSPFLENAVP--EGDEG--KGPESPNIHFEPVVEL-QRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1048 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1127
Cdd:COG5171    81 HLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767919496 1128 AWMW-SASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:COG5171   161 SWVWmSTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1307-1469 1.27e-36

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 138.23  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1307 KLNQSGTSVGTDEESVVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQN 1386
Cdd:COG5171    44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1387 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1465
Cdd:COG5171   123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                  ....
gi 767919496 1466 AQEK 1469
Cdd:COG5171   203 HNEK 206
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 33-222 2.09e-15

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: 78.23  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDG 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  113 RAKYWvERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 767919496  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 60-92 1.03e-04

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: 40.89  E-value: 1.03e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 767919496     60 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
TPR_1 pfam00515
Tetratricopeptide repeat;
60-92 1.06e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 40.87  E-value: 1.06e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767919496    60 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
PRK08581 PRK08581
amidase domain-containing protein;
1504-1680 1.39e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 43.24  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1504 TDVIQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFVSESVKRIFSS----EKSKPFAFGNSSATGSLfgfsfnAPLKS 1579
Cdd:PRK08581   55 TSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTninqLLTKNKYDDNYSLTTLI------QNLFN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1580 NNSETSSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLSAS----FPTEESSINYTFKTPEKGFNFSLFKSNPMAfw 1655
Cdd:PRK08581  129 LNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADnqkaPSSNNTKPSTSNKQPNSPKPTQPNQSNSQP-- 206

                         170       180
                  ....*....|....*....|....*
gi 767919496 1656 TSTPSSQPESKAKEKKKPEDSPSDS 1680
Cdd:PRK08581  207 ASDDTANQKSSSKDNQSMSDSALDS 231
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 30-205 4.33e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.99  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496    30 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAE-LLC 105
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   106 KNDVtdGRAKYWVERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVELYRSTKRLKd 183
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180
                   ....*....|....*....|..
gi 767919496   184 avahchEAERniALRSSLEWNS 205
Cdd:TIGR02917  653 ------KAIT--SLKRALELKP 666
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 33-91 6.01e-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: 40.69  E-value: 6.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNP 91
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 ...
 1348-1464 3.71e-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: 261.82  E-value: 3.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
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 ...
 1051-1167 3.25e-78

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: 253.43  E-value: 3.25e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1348-1464 1.19e-70

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: 231.78  E-value: 1.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD_RanBP2-like cd13176
Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...
 1051-1167 3.63e-69

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: 227.54  E-value: 3.63e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1334-1463 1.37e-63

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: 212.25  E-value: 1.37e-63
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   1334 FEPVVPLPDlVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1412
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767919496   1413 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1463
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
Ran_BP1 pfam00638
RanBP1 domain;
1345-1466 6.78e-63

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 209.98  E-value: 6.78e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  1345 EVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1424
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767919496  1425 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1466
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
Ran_BP1 pfam00638
RanBP1 domain;
1048-1169 1.88e-62

RanBP1 domain;


Pssm-ID: 395513 [Multi-domain]  Cd Length: 122  Bit Score: 208.44  E-value: 1.88e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  1048 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1127
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 767919496  1128 AWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQRL 1169
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1034-1167 1.22e-58

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: 198.18  E-value: 1.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1034 DIHFEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEVR--QWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANH 1111
Cdd:cd13179     1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767919496 1112 WITTTMNLKPLSGSDRAWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13179    80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_RanBP1 cd13179
Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...
 1333-1464 6.39e-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: 190.47  E-value: 6.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1333 YFEPVVPLPdLVEVSSGEENEQVVFSHRAEIYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 1410
Cdd:cd13179     3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767919496 1411 TPDMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13179    82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1051-1167 1.54e-52

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


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 180.10  E-value: 1.54e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1131 WSASDFSD-GDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd00835    81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118
RanBD_family cd00835
Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...
 1348-1464 1.96e-52

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


Pssm-ID: 269907 [Multi-domain]  Cd Length: 118  Bit Score: 179.72  E-value: 1.96e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1428 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
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 ...
 1051-1167 2.95e-51

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


Pssm-ID: 270204  Cd Length: 117  Bit Score: 176.31  E-value: 2.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
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 ...
 1348-1464 7.65e-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: 172.45  E-value: 7.65e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD smart00160
Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...
 1037-1166 7.46e-49

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


Pssm-ID: 197549  Cd Length: 130  Bit Score: 169.88  E-value: 7.46e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   1037 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 1115
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 767919496   1116 TMNLKPLSGSDRAWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEEC 1166
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130
RanBD4_RanBP2-like cd13178
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1167 1.32e-48

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


Pssm-ID: 269999  Cd Length: 117  Bit Score: 168.98  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1167 2.12e-48

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


Pssm-ID: 270203 [Multi-domain]  Cd Length: 117  Bit Score: 168.28  E-value: 2.12e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
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 ...
 1348-1464 1.32e-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 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: 154.43  E-value: 1.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
975-1167 4.16e-43

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 156.72  E-value: 4.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  975 AKSTSGEGFQ-------FGKKDLnfkgFSGAGEKLFSSRYGKMANKANTSGdfEKDDDayKTEDSDDIHFEPVVQMpEKV 1047
Cdd:COG5171    10 AKIEKEENEQkersldvVSKGDA----FGDGKAGGEEKKVQQSPFLENAVP--EGDEG--KGPESPNIHFEPVVEL-QRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1048 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1127
Cdd:COG5171    81 HLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767919496 1128 AWMW-SASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:COG5171   161 SWVWmSTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201
RanBD2_RanBP2_insect-like cd13172
Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1167 4.90e-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: 152.99  E-value: 4.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKN-EVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAW 1129
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1130 MWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
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 ...
 1348-1464 1.27e-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: 151.83  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1426
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1427 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13172    81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1165 1.45e-41

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


Pssm-ID: 269992  Cd Length: 117  Bit Score: 148.77  E-value: 1.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAevRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYVD--KEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEE 1165
Cdd:cd13171    79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTK 113
RanBD1_RanBP2-like cd14684
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1348-1464 6.83e-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: 144.02  E-value: 6.83e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1427
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1348-1464 8.75e-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: 143.39  E-value: 8.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERVWV 1427
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1428 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13173    77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAK 113
RanBD1_RanBP2_insect-like cd13171
Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...
 1348-1464 1.29e-38

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


Pssm-ID: 269992  Cd Length: 117  Bit Score: 140.29  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1426
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1427 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13171    78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1167 2.72e-38

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


Pssm-ID: 269995  Cd Length: 118  Bit Score: 139.46  E-value: 2.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1130
Cdd:cd13174     1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767919496 1131 WSASDFS-DGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13174    81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118
RanBD3_RanBP2_insect-like cd13173
Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...
 1051-1165 2.92e-37

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: 136.46  E-value: 2.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAevRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPlsGSDRAWM 1130
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767919496 1131 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEE 1165
Cdd:cd13173    77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111
YRB1 COG5171
Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion];
1307-1469 1.27e-36

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


Pssm-ID: 227499  Cd Length: 211  Bit Score: 138.23  E-value: 1.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1307 KLNQSGTSVGTDEESVVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQN 1386
Cdd:COG5171    44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1387 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1465
Cdd:COG5171   123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                  ....
gi 767919496 1466 AQEK 1469
Cdd:COG5171   203 HNEK 206
RanBD4_RanBP2_insect-like cd13174
Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...
 1349-1463 1.04e-33

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: 126.37  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1349 GEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVW 1428
Cdd:cd13174     2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767919496 1429 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 1463
Cdd:cd13174    82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1348-1464 3.83e-16

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


Pssm-ID: 269990  Cd Length: 117  Bit Score: 75.95  E-value: 3.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNM--KGTERV 1425
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMggKGVTFA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767919496 1426 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13169    79 CVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1051-1167 1.91e-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: 73.79  E-value: 1.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVrQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDrawm 1130
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKKDDG-EWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1131 wSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13170    76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 33-222 2.09e-15

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: 78.23  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDG 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  113 RAKYWvERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 767919496  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269
RanBD_NUP50 cd13170
Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...
 1349-1464 1.10e-14

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: 71.86  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1349 GEENEQVVFSHRAEIYRYDKDvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMslqNMKGTERVWVW 1428
Cdd:cd13170     2 GEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGM---PYSVAGKNNVF 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767919496 1429 TACDFADGerKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13170    78 VGCVPNPG--KPVTYLLRVKTAEDADELAKALEEEK 111
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1051-1123 2.43e-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: 70.72  E-value: 2.43e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKL--RMLMRREQVLKVCANHWITTTMNLKPLS 1123
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGqsRIVMRTQGSLRVILNTKIWPGMTVEKVS 75
RanBD_NUP50_plant cd13169
Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...
 1051-1165 2.62e-14

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


Pssm-ID: 269990  Cd Length: 117  Bit Score: 70.94  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAevRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLS--GSDRA 1128
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGgkGVTFA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 767919496 1129 WMWSAsdfSDGDAKLERLAAKFKTPELAEEFKQKFEE 1165
Cdd:cd13169    79 CVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEA 112
RanBD_RanBP3 cd13180
Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...
 1348-1459 7.50e-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: 69.57  E-value: 7.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKI--LQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERV 1425
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVE--KVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767919496 1426 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKI 1459
Cdd:cd13180    79 LRITA---MDDEGQVKVFLLQASPEDAKQLYNAI 109
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1051-1167 1.35e-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: 68.62  E-value: 1.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1051 TGEEGEKVLYSQGVKLFRFDAEVRQ--WKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDra 1128
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGS-- 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767919496 1129 wMWSASDFSdGDAKLERLAAKFKTPELAEEFKQKFEECQ 1167
Cdd:cd13181    79 -LVRVPTIN-SDGKIETYVIKVKTAADGEELLKALNDAK 115
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 29-191 3.25e-12

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: 68.99  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   29 GFYF-AKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELL 104
Cdd:COG2956    10 GWYFkGLNYLLNGQPDKAIDL---LEEALELDPEtveAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  105 CKNDVTDgRAKYWVERAAKLFPGSPAIYklkEQLLDC---EGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRL 181
Cdd:COG2956    87 LKAGLLD-RAEELLEKLLELDPDDAEAL---RLLAEIyeqEGD--WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                         170
                  ....*....|
gi 767919496  182 KDAVAHCHEA 191
Cdd:COG2956   161 DEAIEALEKA 170
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-139 5.13e-11

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: 62.13  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDV 109
Cdd:COG4783     8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGD 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 767919496  110 TDGRAKYWvERAAKLFPGSPAIYKLKEQLL 139
Cdd:COG4783    88 YDEALALL-EKALKLDPEHPEAYLRLARAY 116
RanBD_NUP2 cd13181
Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...
 1348-1464 1.38e-10

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: 60.14  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1348 SGEENEQVVFSHRAEIYRYD--KDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERV 1425
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMGNGSLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767919496 1426 WVWTacdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13181    81 RVPT----INSDGKIETYVIKVKTAADGEELLKALNDAK 115
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
30-260 5.42e-10

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 61.56  E-value: 5.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCK-ND 108
Cdd:COG0457    12 NNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAlGR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  109 VTDGRAKYwvERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRLKDAVAHC 188
Cdd:COG0457    92 YEEALEDY--DKALELDPDDAEALYNLGLALLELGR--YDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919496  189 HEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQENRELLE 260
Cdd:COG0457   168 EKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
53-299 3.01e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 56.55  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   53 INVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCK-NDVTDGRAKYwvERAAKLFPGSPAI 131
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRlGRYEEALADY--EQALELDPDDAEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  132 YKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVELYRSTKRLKDAVAHCHEA-ERNIALRSSLEWNSCVVQT 210
Cdd:COG0457    79 LNNLGLALQALGR--YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAlELDPDDADALYNLGIALEK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  211 LKEYLESLQCLEsdkSDWRATNTDLLLAYANLMLLTLSTRDVQENRELLESFDSALQSAKSSLGGNDELSATFLEMKGHF 290
Cdd:COG0457   157 LGRYEEALELLE---KLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLAL 233


                  ....*....
gi 767919496  291 YMYAGSLLL 299
Cdd:COG0457   234 RLAALALYQ 242
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 35-126 1.29e-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: 53.04  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   35 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 114
Cdd:COG5010    63 LYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDD-EA 141

                          90
                  ....*....|..
gi 767919496  115 KYWVERAAKLFP 126
Cdd:COG5010   142 KAALQRALGTSP 153
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 59-132 2.79e-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: 51.16  E-value: 2.79e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919496   59 DPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFPGSPAIY 132
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE-EAEELLERALALDPDNPEAL 88
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
35-126 3.38e-06

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 47.09  E-value: 3.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   35 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVEcYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 114
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD-EA 78

                          90
                  ....*....|..
gi 767919496  115 KYWVERAAKLFP 126
Cdd:COG3063    79 LAYLERALELDP 90
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 31-126 4.54e-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: 47.88  E-value: 4.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   31 YFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVT 110
Cdd:COG4783    43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                          90
                  ....*....|....*.
gi 767919496  111 DGRAKYWvERAAKLFP 126
Cdd:COG4783   123 DEAIAAL-EKALELDP 137
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 30-93 8.32e-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: 47.11  E-value: 8.32e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767919496   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQ 93
Cdd:COG4783    76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 32-269 1.12e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 50.38  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   32 FAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCK-NDVT 110
Cdd:COG3914    84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRlGRLE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  111 DGRAKYwvERAAKLFPGSPAIYklkeqlldcegedgwnklfdliqselyvrpddvhvnIRLVELYRSTKRLKDAVAHCHE 190
Cdd:COG3914   164 EAIAAL--RRALELDPDNAEAL------------------------------------NNLGNALQDLGRLEEAIAAYRR 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496  191 AER----NIALRSSLE---WNSCVVQTLKEYLESLQCLESDKSDWratntdlllayANLMLLTLSTRDVQENRELLESFD 263
Cdd:COG3914   206 ALEldpdNADAHSNLLfalRQACDWEVYDRFEELLAALARGPSEL-----------SPFALLYLPDDDPAELLALARAWA 274


                  ....*.
gi 767919496  264 SALQSA 269
Cdd:COG3914   275 QLVAAA 280
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 34-138 5.77e-05

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


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 44.21  E-value: 5.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   34 KLYYEAKEYDLAKKYictYINVQERDPK------AHRFLGLLYELEENTEKAVECYRRSVELNPTQK---DLVLKIAELL 104
Cdd:COG1729     1 KALLKAGDYDEAIAA---FKAFLKRYPNsplapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSY 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767919496  105 CKNDVTDgRAKYWVERAAKLFPGSPAIYKLKEQL 138
Cdd:COG1729    78 LELGDYD-KARATLEELIKKYPDSEAAKEARARL 110
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 33-91 7.03e-05

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: 44.95  E-value: 7.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNP 91
Cdd:COG5010    95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 30-132 9.73e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.30  E-value: 9.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCK-ND 108
Cdd:COG3914   116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDlGR 195

                          90       100
                  ....*....|....*....|....
gi 767919496  109 VTDGRAKYwvERAAKLFPGSPAIY 132
Cdd:COG3914   196 LEEAIAAY--RRALELDPDNADAH 217
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 60-92 1.03e-04

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: 40.89  E-value: 1.03e-04
                            10        20        30
                    ....*....|....*....|....*....|...
gi 767919496     60 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
TPR_1 pfam00515
Tetratricopeptide repeat;
60-92 1.06e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 40.87  E-value: 1.06e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767919496    60 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 30-91 2.24e-04

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: 42.69  E-value: 2.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767919496   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNP 91
Cdd:COG4235    55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLP 116
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 60-92 3.33e-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: 39.43  E-value: 3.33e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767919496    60 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 33-89 9.66e-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: 43.36  E-value: 9.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINvQERDPKAHRFLGLLYELEENTEKAVECYRRSVEL 89
Cdd:COG3071   265 GRLCLRNQLWGKAREYLEAALA-LRPSAEAYAELARLLEQLGDPEEAAEHYRKALAL 320
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
69-144 1.25e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767919496   69 LYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDGRAKYwvERAAKLFPGSPAIYKLKEQLLDCEGE 144
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIAL--EKALKLDPNNAEALLNLAELLLELGD 74
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
33-91 1.35e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 39.77  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919496   33 AKLYYEAKEYDLAKKYIcTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNP 91
Cdd:COG3063    33 GLLLLEQGRYDEAIALE-KALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDP 90
PRK08581 PRK08581
amidase domain-containing protein;
1504-1680 1.39e-03

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 43.24  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1504 TDVIQGDDVADAASEVEVSSTSETTTKAVVSPPKFVFVSESVKRIFSS----EKSKPFAFGNSSATGSLfgfsfnAPLKS 1579
Cdd:PRK08581   55 TSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTninqLLTKNKYDDNYSLTTLI------QNLFN 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1580 NNSETSSVAQSGSESKVEPKKCELSKNSDIEQSSDSKVKNLSAS----FPTEESSINYTFKTPEKGFNFSLFKSNPMAfw 1655
Cdd:PRK08581  129 LNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTQSSKQDKADnqkaPSSNNTKPSTSNKQPNSPKPTQPNQSNSQP-- 206

                         170       180
                  ....*....|....*....|....*
gi 767919496 1656 TSTPSSQPESKAKEKKKPEDSPSDS 1680
Cdd:PRK08581  207 ASDDTANQKSSSKDNQSMSDSALDS 231
RanBD5_RanBP2_insect-like cd13175
Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ...
 1350-1464 1.72e-03

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: 39.83  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496 1350 EENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSlqnMKGTERVWVWT 1429
Cdd:cd13175     3 DDEELFMFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEIYGARIVLSDDDTDTIIANTIIAVQTS---LRVEGKEAIWS 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767919496 1430 ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1464
Cdd:cd13175    80 AIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK 114
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
35-92 1.75e-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: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767919496   35 LYYEAKEYDLAkkyICTYINVQERDPK---AHRFLGLLYELEENTEKAVECYRRSVELNPT 92
Cdd:COG4785    82 AYDSLGDYDLA---IADFDQALELDPDlaeAYNNRGLAYLLLGDYDAALEDFDRALELDPD 139
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 52-139 4.01e-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: 39.94  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   52 YINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWVERAAKLFPGSPAI 131
Cdd:COG5010    46 GRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKD-EAKEYYEKALALSPDNPNA 124


                  ....*...
gi 767919496  132 YKLKEQLL 139
Cdd:COG5010   125 YSNLAALL 132
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 30-205 4.33e-03

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.99  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496    30 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAE-LLC 105
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767919496   106 KNDVtdGRAKYWVERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVELYRSTKRLKd 183
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180
                   ....*....|....*....|..
gi 767919496   184 avahchEAERniALRSSLEWNS 205
Cdd:TIGR02917  653 ------KAIT--SLKRALELKP 666
ACL4-like cd24142
Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...
 33-91 6.01e-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: 40.69  E-value: 6.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767919496   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTEKAVECYRRSVELNP 91
Cdd:cd24142     7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65
 
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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