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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1993187848 1644 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1687
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1285 EVSSGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1364
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1993187848 1365 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1406
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

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

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848   977 FEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG-KPRMLMRRDQVLKVCANHWITT 1055
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1993187848  1056 TMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEEC 1106
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1247 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQN 1326
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1327 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1405
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202

                   ....
gi 1993187848 1406 AQEK 1409
Cdd:COG5171    203 HNEK 206

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

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1993187848 1644 AANVEHLKNVLLQFIFLKPGSERESLLPVINTMLQLSPEEKGKL 1687
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44

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

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1993187848  1645 ANVEHLKNVLLQFIFLKPgSERESLLPVINTMLQLSPEEKGKLAAV 1690
Cdd:smart00755    2 ANFEYLKNVLLQFLTLRE-SERETLLPVISTVLQLSPEEMQKLLEV 46

Tetratricopeptide repeat;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1993187848   59 PRAHRFLGLLYELEENTEKAVECYRRSLELNP 90
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNP 32

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848   16 QGSAPSPGKKLRGFYFAKlyyeaKEYDLAKKYVCTYLSVQERDPRAHRFLGLLYELEENTEKAVECYRRSLELNPPQKDL 95
Cdd:TIGR02917  461 QPDNASLHNLLGAIYLGK-----GDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRA 535

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848   96 VLKIAELLCKNDVTDgRAKYWVERAAKLFPG--SPAIYKLKEHLLDCE---GEDGWNKLFDWI--QSELYEYLESLQCLE 168
Cdd:TIGR02917  536 ILALAGLYLRTGNEE-EAVAWLEKAAELNPQeiEPALALAQYYLGKGQlkkALAILNEAADAApdSPEAWLMLGRAQLAA 614

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1993187848  169 SDKSDWRATNTDLL-------LAYAnlmLLTLSTRDVQESRELLESFDSALQ 213
Cdd:TIGR02917  615 GDLNKAVSSFKKLLalqpdsaLALL---LLADAYAVMKNYAKAITSLKRALE 663

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1285 EVSSGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTER 1364
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1993187848 1365 VWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 1406
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  974 DIHFEPVVQMPEkVELVTGEEGEKVLYSQGVKLFRFDAEIS--QWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANH 1051
Cdd:cd13179      1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1993187848 1052 WITTTMNLKPLSGSDRAWMWLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13179     80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1367
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1993187848 1368 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPLSGSDRAWM 1070
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEECQ 1107
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1367
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1368 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1366
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1993187848 1367 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERVWV 1367
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1993187848 1368 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAK 113

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVW 1366
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1993187848 1367 VWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd13171     78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAeiSQWKERGLGNLKILKNEVNGKPRMLMRRDQVLKVCANHWITTTMNLKPlsGSDRAWM 1070
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1993187848 1071 WLASDFSDGDAKLERLAAQFKTPELAEEFKQKFEE 1105
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111

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

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1993187848 1581 EPPLWHAEFTKEELVQKLSSTTKSADQLNGLLRETEATSAVLMEQIKLLKSEIRRLERNQE 1641
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQE 61

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993187848 1288 SGEENEQVVFSHMAELYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNM--KGTERV 1365
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMggKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1993187848 1366 WVWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1404
Cdd:cd13169     79 CVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114

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.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1993187848  991 TGEEGEKVLYSQGVKLFRFDAEISQWKERGLGNLKILKNEVNG--KPRMLMRRDQVLKVCANHWITTTMNLKPLS 1063
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGsgQSRIVMRTQGSLRVILNTKIWPGMTVEKVS 75