cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2893 PVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKG-----FGFKNSIFHRVVPDFICQGGDITKYNGTGGQSI 2967
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2968 YGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICI 3047
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160

                  ....
gi 153792534 3048 TECG 3051
Cdd:cd01926   161 ADCG 164

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 153792534 1180 TGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1259
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 1260 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1296
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 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 153792534 2754 SGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALV 2833
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 2834 WTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQ 2870
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00638, pfam00641, pfam00160. There are two conserved sequence motifs: TFFC and EDF. Nup358/RanBP2 is a nucleoporin involved in ubiquitination of many different protein targets from various cellular pathways. It complexes with Ubc9, SUMO-1 and RanGAP1 to perform this function. This is the ligase domain which binds to Ubc9.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792534  2468 DILIVYELTPTPEQKALAEKLLLPSTFFCyknrpGYVSEEEEDDEDY--EMAVKKLNGKLYLDDS 2530
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

Zn-finger in Ran binding protein and others;

                           10        20        30
                   ....*....|....*....|....*....|
gi 153792534  1469 KEGQWECSVCLVRNERSAKKCVACENPGKQ 1498
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

Zn-finger in Ran binding protein and others;

                           10        20
                   ....*....|....*....|....*....
gi 153792534  1410 KEGHWDCSVCLVRNEPTVSRCIACQNTKS 1438
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

Zn-finger in Ran binding protein and others;

                           10        20        30
                   ....*....|....*....|....*....|
gi 153792534  1345 KEGpYWNCNSCSFKNAATAKKCVSCQNTNP 1374
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKP 29

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2893 PVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKG-----FGFKNSIFHRVVPDFICQGGDITKYNGTGGQSI 2967
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2968 YGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICI 3047
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160

                  ....
gi 153792534 3048 TECG 3051
Cdd:cd01926   161 ADCG 164

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 153792534 1180 TGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1259
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 1260 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1296
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 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 153792534 2754 SGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALV 2833
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 2834 WTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQ 2870
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534  1177 EVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDR 1256
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 153792534  1257 SFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQNI 1298
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534  1861 ELVTGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 1940
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 153792534  1941 AWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRL 1982
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBP1 domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534  2158 EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQTMKGTER 2237
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 153792534  2238 VWVWTACDFADGERKIEHLAVRFKLQDVADSFKKIFDEAKTA 2279
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 153792534   1166 FEPVVPLPDkIEVKTGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSG-KIRLLMRREQVLKICANHYISP 1244
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 153792534   1245 DMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1295
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534  2906 LGRIIMELFSNIVPQTAENFRALCTgeKGFgFKNSIFHRVVPDFICQGGDITkynGTGGQSIYGDKFDDENFD--LKHtG 2983
Cdd:pfam00160    6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-K 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792534  2984 PGLLSMANYGQ--NTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESfGSPKGSV-SRRICITECG 3051
Cdd:pfam00160   79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEK-VPTDGDRpVKPVKILSCG 148

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 1799 GKKDPNFKGFSGAGEKLF--SSQSGKVAEKANTSSDLEK---DDDAYKTEDSDDIHFEPVVQMpEKVELVTGEEDEKVLY 1873
Cdd:COG5171    15 EENEQKERSLDVVSKGDAfgDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 1874 SQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMWL-ASDFSDG 1952
Cdd:COG5171    94 KARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEG 173

                         170       180
                  ....*....|....*....|....*...
gi 153792534 1953 DAKLEQLAAKFKTPELAEEFKQKFEECQ 1980
Cdd:COG5171   174 EAKAQTFAIRFYSEENAKRFKEEFEKGQ 201

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2890 DTNPVVFFDVcadgePLGRIIMELFSNIVPQTAENFRALCtgEKGFgFKNSIFHRVVPDFICQGGDITkYNGTGGQsiyG 2969
Cdd:COG0652     4 APNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---G 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792534 2970 DKFDDENF-DLKHTgPGLLSMAN-YGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIES 3033
Cdd:COG0652    72 YTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is approximately 60 amino acids in length. The family is found in association with pfam00638, pfam00641, pfam00160. There are two conserved sequence motifs: TFFC and EDF. Nup358/RanBP2 is a nucleoporin involved in ubiquitination of many different protein targets from various cellular pathways. It complexes with Ubc9, SUMO-1 and RanGAP1 to perform this function. This is the ligase domain which binds to Ubc9.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792534  2544 ECVIVWEKKPTVEERAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELRKVCEAQKSQNE 2604
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLYPDDE 60

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534   33 AKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAVECYKRSVELNPTQKDLVLKIAELLCKNDVTDG 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDE 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534  113 RAKYWvERAAKLFPGSPAIYKLKEQLLDCKGEdgWNKLFDLIQSELYARPDDIHVNIRLVELYRSNKRLKDAVAHCHEAD 192
Cdd:COG2956   163 AIEAL-EKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180
                  ....*....|....*....|....*....
gi 153792534  193 RNTALRSSLEWNLCVVQTLKEYLESLQCL 221
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALL 268

Zn-finger in Ran binding protein and others;

                           10        20
                   ....*....|....*....|....*....
gi 153792534  1617 KEGEWECAVCSVQNESSSLKCVACEASKP 1645
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

Zn-finger in Ran binding protein and others;

                           10        20        30
                   ....*....|....*....|....*....|
gi 153792534  1558 KEGQWDCSLCFVRNEASATHCIACQYPNKQ 1587
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.

                            10        20
                    ....*....|....*....|....*
gi 153792534   1471 GQWECSVCLVRNERSAKKCVACENP 1495
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.

                            10        20
                    ....*....|....*....|....*
gi 153792534   1619 GEWECAVCSVQNESSSLKCVACEAS 1643
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

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.

                            10        20        30
                    ....*....|....*....|....*....|...
gi 153792534     60 PKAHRFLGLLYEVEENIDKAVECYKRSVELNPT 92
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.

                            10        20
                    ....*....|....*....|....
gi 153792534   1501 EWHCSLCSVKNEAHAIKCVACNNP 1524
Cdd:smart00547    2 DWECPACTFLNFASRSKCFACGAP 25

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.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792534   33 AKLYYEAKEYDLAKKYISTYINVQERDPKAHRFLGLLYEVEENIDKAVECYKRSVELNP 91
Cdd:cd24142     7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.

                            10        20
                    ....*....|....*....|..
gi 153792534   1350 WNCNSCSFKNAATAKKCVSCQN 1371
Cdd:smart00547    3 WECPACTFLNFASRSKCFACGA 24

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2893 PVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGEKG-----FGFKNSIFHRVVPDFICQGGDITKYNGTGGQSI 2967
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2968 YGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKGSVSRRICI 3047
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160

                  ....
gi 153792534 3048 TECG 3051
Cdd:cd01926   161 ADCG 164

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 153792534 1180 TGEEDEEEFFCNRAKLFRFDGESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1259
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 1260 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1296
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 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 153792534 2754 SGEEDEEVLFKERAKLYRWDRDVSQWKERGIGDIKILWHTMKKYYRILMRRDQVFKVCANHVITKAMELKPLNVSNNALV 2833
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 2834 WTASDYADGEAKVEQLAVRFKTKEMTESFKKKFEECQ 2870
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

cyclophilin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2886 ELSKdtNPVVFFDVCADGEPLGRIIMELFSNIVPQTAENFRALCTGE------KGFGFKNSIFHRVVPDFICQGGDITKY 2959
Cdd:PTZ00060   11 EMSK--RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792534 2960 NGTGGQSIYGDKFDDENFDLKHTGPGLLSMANYGQNTNSSQFFITLKKAEHLDFKHVVFGFVKDGMDTVRKIESFGSPKG 3039
Cdd:PTZ00060   89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG 168

                         170
                  ....*....|....
gi 153792534 3040 SVSRRICITECGQL 3053
Cdd:PTZ00060  169 YPKKPVVVTDCGEL 182

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 153792534 1864 TGEEDEKVLYSQRVKLFRFDAEISQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 1943
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 153792534 1944 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 1980
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

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 153792534 1163 GPHFEPVVPLPdKIEVKTGEEDEEEFFCNRAKLFRFD--GESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANH 1240
Cdd:cd13179     1 DAQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDteNDPPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 153792534 1241 YISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1296
Cdd:cd13179    80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135