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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

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 1859470548 1615 EPPLWHAEFTKEELVQKLRSTTKSADHLNGLLREIEATNAVLMEQIKLLKSEIRRLERNQEREKS 1679
Cdd:pfam16704    1 EPFVWTVEPSKSELTQKLSTTTKSADHLNGLLRETEATNAILMEQIKLLKSEIRRLERNQEREKS 65

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 1859470548 1680 AANLEYLKNVLLQFIFLKPGSERERLLPVINTMLQLSPEEKGKL 1723
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include 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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

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 1859470548  1308 FEPVVPLPDlVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1386
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1859470548  1387 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1437
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1022 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1101
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1859470548 1102 AWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQRL 1143
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548  949 AKSTSGEGFQ-------FGKKDLnfkgFSGAGEKLFSSRYGKMANKANTSGdfEKDDDayKTEDSDDIHFEPVVQMpEKV 1021
Cdd:COG5171     10 AKIEKEENEQkersldvVSKGDA----FGDGKAGGEEKKVQQSPFLENAVP--EGDEG--KGPESPNIHFEPVVEL-QRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1022 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1101
Cdd:COG5171     81 HLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDR 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1859470548 1102 AWMW-SASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1141
Cdd:COG5171    161 SWVWmSTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201

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

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1281 KLNQSGTSVGTDEESVVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQN 1360
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1361 YDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 1439
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202

                   ....
gi 1859470548 1440 AQEK 1443
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 1859470548 1680 AANLEYLKNVLLQFIFLKPGSERERLLPVINTMLQLSPEEKGKL 1723
Cdd:pfam01465    1 GANLEYLKNVLLQFLESKESSERKQLLPVIATLLKFSPEEEQKI 44

Tetratricopeptide repeat;

                           10        20        30
                   ....*....|....*....|....*....|...
gi 1859470548   34 PKAHRFLGLLYELEENTEKAVECYRRSVELNPT 66
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33

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 1859470548    4 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTEKAVECYRRSVELNPTQKDLVLKIAE-LLC 79
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548   80 KNDVtdGRAKYWVERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVELYRSTKRLKd 157
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180
                   ....*....|....*....|..
gi 1859470548  158 avahchEAERniALRSSLEWNS 179
Cdd:TIGR02917  653 ------KAIT--SLKRALELKP 666

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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

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 1859470548  1308 FEPVVPLPDlVEVSSGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 1386
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1859470548  1387 DMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 1437
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1022 ELVTGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1101
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1859470548 1102 AWMWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQRL 1143
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 1859470548 1307 YFEPVVPLPdLVEVSSGEENEQVVFSHRAEIYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 1384
Cdd:cd13179      3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1859470548 1385 TPDMSLQNMKGTERVWVWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd13179     82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1859470548 1402 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 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 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1104
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1105 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1141
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWV 1401
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
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 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKN-EVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAW 1103
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1859470548 1104 MWSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1141
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

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 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAevRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1104
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVD--KEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1859470548 1105 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEE 1139
Cdd:cd13171     79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTK 113

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 1859470548 1322 SGEENEQVVFSHRAEIYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQnmKGTERVWV 1401
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1402 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 1438
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAK 113

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAEVRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1104
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1859470548 1105 WSASDFS-DGDAKLERLAAKFKTPELAEEFKQKFEECQ 1141
Cdd:cd13174     81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 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 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAevRQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPlsGSDRAWM 1104
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1859470548 1105 WSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEE 1139
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1323 GEENEQVVFSHRAEIYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMSLQNMKGTERVWVW 1402
Cdd:cd13174      2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1859470548 1403 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 1437
Cdd:cd13174     82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1859470548 1025 TGEEGEKVLYSQGVKLFRFDAEVrQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDrawm 1104
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKKDDG-EWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1859470548 1105 wSASDFSDGDAKLERLAAKFKTPELAEEFKQKFEECQ 1141
Cdd:cd13170     76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111