NCBI Conserved Domain Search

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

1.10e-83

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

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 269.99 E-value: 1.10e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

4.03e-83

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

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 268.44 E-value: 4.03e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

1.63e-82

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

Pssm-ID: 270204 Cd Length: 117 Bit Score: 266.83 E-value: 1.63e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

2.20e-82

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

Pssm-ID: 269999 Cd Length: 117 Bit Score: 266.43 E-value: 2.20e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

IR1-M

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2734-2790

4.51e-28

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.

Pssm-ID: 463488 Cd Length: 60 Bit Score: 108.71 E-value: 4.51e-28

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575772 2734 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQY 2790
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLY 56

LapB

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...

32-221

4.50e-16

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

Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 81.31 E-value: 4.50e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   32 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  112 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 191
Cdd:COG2956    162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462575772  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

IR1-M super family

cl13601

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2656-2718

3.03e-15

The actual alignment was detected with superfamily member pfam12185:

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 3.03e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 2656 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2718
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

zf-RanBP

Zn-finger in Ran binding protein and others;

1780-1808

6.59e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.59e-11

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1780 RKGQWDCSVCCVQNESSSLKCVACDASKP 1808
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1478-1507

1.34e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.34e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1478 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1507
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1664-1693

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1664 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1693
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1605-1634

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1605 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1634
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1542-1571

5.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1542 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1571
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1723-1752

1.26e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.26e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1723 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1752
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1414-1442

3.08e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.08e-08

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1414 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1442
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1350-1380

7.87e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.87e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462575772 1350 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1380
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKPD 30

Name

Accession

Description

Interval

E-value

cyclophilin_ABH_like

cd01926

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...

3097-3255

3.88e-94

Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 301.87 E-value: 3.88e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3097 PVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKG-----FGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSI 3171
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3172 YGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITI 3251
Cdd:cd01926     81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                   ....
gi 2462575772 3252 TECG 3255
Cdd:cd01926    161 ADCG 164

RanBD2_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

1.10e-83

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 269.99 E-value: 1.10e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

4.03e-83

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 268.44 E-value: 4.03e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

1.63e-82

Pssm-ID: 270204 Cd Length: 117 Bit Score: 266.83 E-value: 1.63e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

2.20e-82

Pssm-ID: 269999 Cd Length: 117 Bit Score: 266.43 E-value: 2.20e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

PTZ00060

cyclophilin; Provisional

3090-3257

8.60e-72

cyclophilin; Provisional

Pssm-ID: 240249 Cd Length: 183 Bit Score: 238.59 E-value: 8.60e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3090 ELSKetNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE------KGFGFKNSIFHRVIPDFVCQGGDITKH 3163
Cdd:PTZ00060    11 EMSK--RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNH 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3164 DGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3243
Cdd:PTZ00060    89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG 168

                          170
                   ....*....|....
gi 2462575772 3244 SVCRRITITECGQI 3257
Cdd:PTZ00060   169 YPKKPVVVTDCGEL 182

Ran_BP1

RanBP1 domain;

2955-3076

4.04e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.77 E-value: 4.04e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2955 EVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNN 3034
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 3035 ALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3076
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

1182-1303

6.01e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.00 E-value: 6.01e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1182 EVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDR 1261
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 1262 SFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1303
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

2023-2144

9.99e-67

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 221.53 E-value: 9.99e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2023 ELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 2102
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 2103 AWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRL 2144
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2945-3073

2.25e-66

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 221.11 E-value: 2.25e-66

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2945 FEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMK-NYYRILMRRDQVFKVCANHVITKT 3023
Cdd:smart00160    1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFKS 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 2462575772  3024 MELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC 3073
Cdd:smart00160   81 MTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Ran_BP1

RanBP1 domain;

2320-2441

2.72e-65

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 217.68 E-value: 2.72e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2320 EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER 2399
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 2400 VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 2441
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2309-2438

2.90e-65

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 217.64 E-value: 2.90e-65

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2309 FEPVVPLPDlVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 2387
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  2388 DMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 2438
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

1171-1300

3.05e-54

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 186.44 E-value: 3.05e-54

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  1171 FEPVVPLPDkIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSG-KIRLLMRREQVLKICANHYISP 1249
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  1250 DMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1300
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2012-2141

9.38e-52

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 179.12 E-value: 9.38e-52

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2012 FEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 2090
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  2091 TMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEEC 2141
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Pro_isomerase

pfam00160

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...

3110-3255

9.83e-49

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.

Pssm-ID: 459694 [Multi-domain] Cd Length: 149 Bit Score: 171.28 E-value: 9.83e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITkhdGTGGQSIYGDKFEDENFDVKHT-GP 3188
Cdd:pfam00160    6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPLLLKhKR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3189 GLLSMANQGQ--NTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESfGSPKGSV-CRRITITECG 3255
Cdd:pfam00160   80 GALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEK-VPTDGDRpVKPVKILSCG 148

YRB1

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

1950-2142

3.08e-45

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 163.65 E-value: 3.08e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1950 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQYGKMANKANTSGDFEK---DDDAYKTEDSDDIHFEPVVQMpEKVELVT 2026
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2027 GEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMW 2106
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462575772 2107 L-ASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:COG5171    165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201

YRB1

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

2882-3082

1.16e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 159.41 E-value: 1.16e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2882 SFADLASSNSGDfAFGSKDKNFQWANTGAAVFGTQsvgtqsagKVGEDEDGSDEEvvhNEDIHFEPIVSLPEVEVKSGEE 2961
Cdd:COG5171     20 KERSLDVVSKGD-AFGDGKAGGEEKKVQQSPFLEN--------AVPEGDEGKGPE---SPNIHFEPVVELQRVHLKTNEE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2962 DEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWT-A 3040
Cdd:COG5171     88 DETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsT 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 3041 SDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQK 3082
Cdd:COG5171    168 ADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALK 209

YRB1

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

1170-1303

2.30e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 158.26 E-value: 2.30e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1170 HFEPVVPLpDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISP 1249
Cdd:COG5171     70 HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINP 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 1250 DMKLTPNAGSDRSFVWH-ALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1303
Cdd:COG5171    149 EFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEH 203

PpiB

COG0652

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...

3094-3237

2.88e-40

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

Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 147.62 E-value: 2.88e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3094 ETNPVVFFDVcadgePLGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQsiyG 3173
Cdd:COG0652      4 APNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---G 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 3174 DKFEDENF-DVKHTgPGLLSMAN-QGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIES 3237
Cdd:COG0652     72 YTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136

YRB1

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

2282-2444

5.85e-39

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 145.93 E-value: 5.85e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2282 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN 2361
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2362 YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 2440
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 2462575772 2441 AQEK 2444
Cdd:COG5171    203 HNEK 206

IR1-M

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2734-2790

4.51e-28

Pssm-ID: 463488 Cd Length: 60 Bit Score: 108.71 E-value: 4.51e-28

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575772 2734 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQY 2790
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLY 56

LapB

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...

32-221

4.50e-16

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

Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 81.31 E-value: 4.50e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   32 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  112 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 191
Cdd:COG2956    162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462575772  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

IR1-M

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2656-2718

3.03e-15

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 3.03e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 2656 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2718
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

zf-RanBP

Zn-finger in Ran binding protein and others;

1780-1808

6.59e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.59e-11

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1780 RKGQWDCSVCCVQNESSSLKCVACDASKP 1808
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1478-1507

1.34e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.34e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1478 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1507
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1664-1693

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1664 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1693
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1605-1634

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1605 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1634
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1542-1571

5.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1542 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1571
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1723-1752

1.26e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.26e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1723 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1752
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1414-1442

3.08e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.08e-08

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1414 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1442
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1350-1380

7.87e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.87e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462575772 1350 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1380
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKPD 30

ZnF_RBZ

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

1666-1690

6.81e-06

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 45.00 E-value: 6.81e-06

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1666 GQWDCSVCLVRNEASATKCIACQNP 1690
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1607-1631

6.81e-06

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 45.00 E-value: 6.81e-06

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1607 GQWDCSVCLVRNEASATKCIACQNP 1631
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1725-1747

5.17e-05

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 42.30 E-value: 5.17e-05

                            10        20
                    ....*....|....*....|...
gi 2462575772  1725 GQWDCSVCLVRNEASATKCIACQ 1747
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23

ZnF_RBZ

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

1782-1806

7.51e-05

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.92 E-value: 7.51e-05

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1782 GQWDCSVCCVQNESSSLKCVACDAS 1806
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1480-1504

1.35e-04

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 1.35e-04

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1480 GQWDCSACLVQNEGSSTKCAACQNP 1504
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR

smart00028

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...

59-91

1.37e-04

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.

Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 41.28 E-value: 1.37e-04

                            10        20        30
                    ....*....|....*....|....*....|...
gi 2462575772    59 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 91
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33

ZnF_RBZ

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

1544-1568

1.51e-04

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 1.51e-04

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1544 GQWDCSSCLVRNEANATRCVACQNP 1568
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR_1

pfam00515

Tetratricopeptide repeat;

59-91

1.76e-04

Tetratricopeptide repeat;

Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 40.87 E-value: 1.76e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462575772   59 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 91
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33

PEP_TPR_lipo

TIGR02917

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...

29-290

1.93e-04

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

Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.39 E-value: 1.93e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAE-LLC 104
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  105 KNDVtdGRAKYWLERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVEVYRSTKRLKd 182
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  183 avahchEAERniALRSSLEWnscvvqtlkeyleslqclesdKSDwratNTDLLLAYANLMLLTlstrdvqesrellQSFD 262
Cdd:TIGR02917  653 ------KAIT--SLKRALEL---------------------KPD----NTEAQIGLAQLLLAA-------------KRTE 686

                          250       260
                   ....*....|....*....|....*...
gi 2462575772  263 SALQSVKSLGGNDELSATFLEMKGHFYM 290
Cdd:TIGR02917  687 SAKKIAKSLQKQHPKAALGFELEGDLYL 714

ZnF_RBZ

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

1416-1439

1.10e-03

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 38.45 E-value: 1.10e-03

                            10        20
                    ....*....|....*....|....
gi 2462575772  1416 GHWDCSICLVRNEPTVSRCIACQN 1439
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGA 24

ACL4-like

cd24142

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 ...

32-90

6.55e-03

Assembly chaperone of ribosomal protein L4 and similar proteins; Assembly chaperone of RPL4 (ACL4) acts as a chaperone for the L4 ribosomal subunit, encoded by RPL4A and RPL4B, and is required for hierarchical ribosome assembly. It is required for the soluble expression of newly synthesized RPL4 and for the protection of RPL4 from the Tom1-dependent cellular degradation machinery. ACL4 shields ribosomal protein L4 until timely release and insertion into the pre-ribosome is possible, once ribosomal protein L18 is present.

Pssm-ID: 467942 [Multi-domain] Cd Length: 306 Bit Score: 41.46 E-value: 6.55e-03

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575772   32 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 90
Cdd:cd24142      7 AEELLDQGNFELALKFLQRALELEPNNVEALELLGEILLELGDVEEAREVLLRAIELDP 65

Name

Accession

Description

Interval

E-value

cyclophilin_ABH_like

cd01926

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...

3097-3255

3.88e-94

Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 301.87 E-value: 3.88e-94

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3097 PVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKG-----FGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSI 3171
Cdd:cd01926      1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3172 YGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITI 3251
Cdd:cd01926     81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                   ....
gi 2462575772 3252 TECG 3255
Cdd:cd01926    161 ADCG 164

RanBD2_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

1.10e-83

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 269.99 E-value: 1.10e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

4.03e-83

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 268.44 E-value: 4.03e-83

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

1.63e-82

Pssm-ID: 270204 Cd Length: 117 Bit Score: 266.83 E-value: 1.63e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

2.20e-82

Pssm-ID: 269999 Cd Length: 117 Bit Score: 266.43 E-value: 2.20e-82

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD_RanBP2-like

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...

2958-3074

5.46e-75

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

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 245.26 E-value: 5.46e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...

1185-1301

5.85e-75

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 244.88 E-value: 5.85e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...

2026-2142

1.00e-73

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 241.41 E-value: 1.00e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

Ran-binding protein 2, Ran binding domains; RanBP2 (also called E3 SUMO-protein ligase RanBP2, ...

2323-2439

1.30e-72

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 238.33 E-value: 1.30e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd13176      1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13176     81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

PTZ00060

cyclophilin; Provisional

3090-3257

8.60e-72

cyclophilin; Provisional

Pssm-ID: 240249 Cd Length: 183 Bit Score: 238.59 E-value: 8.60e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3090 ELSKetNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE------KGFGFKNSIFHRVIPDFVCQGGDITKH 3163
Cdd:PTZ00060    11 EMSK--RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNH 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3164 DGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3243
Cdd:PTZ00060    89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG 168

                          170
                   ....*....|....
gi 2462575772 3244 SVCRRITITECGQI 3257
Cdd:PTZ00060   169 YPKKPVVVTDCGEL 182

RanBD_RanBP1

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...

1169-1301

2.00e-70

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not activate GTPase activity of Ran, but does markedly increase GTP hydrolysis by the RanGTPase-activating protein (RanGAP1). In both mammalian cells and in yeast, RanBP1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran. In addition to Ran, RanBP1 has been shown to interact with Exportin-1 and Importin subunit beta-1 which docks the NPC at the cytoplasmic side of the nuclear pore complex. RabBP1 contains a single RanBD. The RanBD is present in RanBD1, RanBD2, RanBD3, Nuc2, and Nuc50. Most of these proteins have a single RanBD, with the exception of RanBD2 which has 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. The Ran-binding domain is found in multiple copies in Nuclear pore complex proteins. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 232.84 E-value: 2.00e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1169 PHFEPVVPLPdKIEVKTGEEDEEEFFCNRAKLFRFD--VESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHY 1246
Cdd:cd13179      2 AQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDteNDPPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 1247 ISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13179     81 ITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

Ran_BP1

RanBP1 domain;

2955-3076

4.04e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.77 E-value: 4.04e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2955 EVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNN 3034
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 3035 ALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3076
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

1182-1303

6.01e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.00 E-value: 6.01e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1182 EVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDR 1261
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 1262 SFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1303
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

2023-2144

9.99e-67

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 221.53 E-value: 9.99e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2023 ELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 2102
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 2103 AWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRL 2144
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2945-3073

2.25e-66

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 221.11 E-value: 2.25e-66

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2945 FEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMK-NYYRILMRRDQVFKVCANHVITKT 3023
Cdd:smart00160    1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFKS 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 2462575772  3024 MELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC 3073
Cdd:smart00160   81 MTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

PLN03149

peptidyl-prolyl isomerase H (cyclophilin H); Provisional

3096-3257

6.92e-66

peptidyl-prolyl isomerase H (cyclophilin H); Provisional

Pssm-ID: 178694 Cd Length: 186 Bit Score: 222.02 E-value: 6.92e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3096 NPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE---KGF--GFKNSIFHRVIPDFVCQGGDITKHDGTGGQS 3170
Cdd:PLN03149    18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3171 IYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFV-KDGMDTVKKIESFGS-----PKGS 3244
Cdd:PLN03149    98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATgpnnrPKLA 177

                          170
                   ....*....|...
gi 2462575772 3245 VcrriTITECGQI 3257
Cdd:PLN03149   178 C----VISECGEM 186

Ran_BP1

RanBP1 domain;

2320-2441

2.72e-65

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 217.68 E-value: 2.72e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2320 EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER 2399
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 2400 VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 2441
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2309-2438

2.90e-65

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 217.64 E-value: 2.90e-65

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2309 FEPVVPLPDlVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 2387
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  2388 DMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 2438
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD_RanBP1

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...

2942-3075

6.74e-63

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 211.27 E-value: 6.74e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2942 DIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVS--QWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHV 3019
Cdd:cd13179      1 DAQFEPIVKLPEVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHY 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 3020 ITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQ 3075
Cdd:cd13179     81 ITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQK 136

RanBD_RanBP1

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...

2009-2142

1.53e-61

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 207.42 E-value: 1.53e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2009 DIHFEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVS--QWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANH 2086
Cdd:cd13179      1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 2087 WITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13179     80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

RanBD_family

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...

1185-1301

5.12e-59

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

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 199.36 E-value: 5.12e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1265 WHALDYAD-ELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD_RanBP1

Ran-binding domain; RanBP1 interacts specifically with GTP-charged Ran. RanBP1 does not ...

2308-2439

9.11e-57

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 193.55 E-value: 9.11e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2308 YFEPVVPLPdLVEVSSGEENEQVVFSHRAKLYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 2385
Cdd:cd13179      3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462575772 2386 TPDMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13179     82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

RanBD_family

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...

2323-2439

5.42e-55

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 187.80 E-value: 5.42e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2403 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD_family

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...

2026-2142

7.61e-55

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 187.42 E-value: 7.61e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2106 WLASDFSD-GDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

1171-1300

3.05e-54

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 186.44 E-value: 3.05e-54

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  1171 FEPVVPLPDkIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSG-KIRLLMRREQVLKICANHYISP 1249
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  1250 DMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1300
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

cyclophilin

cd00317

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...

3111-3252

5.81e-54

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.

Pssm-ID: 238194 [Multi-domain] Cd Length: 146 Bit Score: 186.32 E-value: 5.81e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3111 GRITMELFSNIVPRTAENFRALCTGEkgfGFKNSIFHRVIPDFVCQGGDITkhDGTGGQSIYGDKFEDENFDVK-HTGPG 3189
Cdd:cd00317      7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyHHRRG 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575772 3190 LLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFG-SPKGSVCRRITIT 3252
Cdd:cd00317     82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTIS 145

RanBD_family

Ran-binding domain; The RanBD is present in RanBP1, RanBP2, RanBP3, Nuc2, and Nuc50. Most of ...

2958-3074

5.26e-53

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 182.41 E-value: 5.26e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd00835      1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 3038 WTASDYAD-GEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd00835     81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

6.19e-53

Pssm-ID: 270204 Cd Length: 117 Bit Score: 182.09 E-value: 6.19e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

4.13e-52

Pssm-ID: 269999 Cd Length: 117 Bit Score: 179.77 E-value: 4.13e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD

Ran-binding domain; Domain of apporximately 150 residues that stabilises the GTP-bound form of ...

2012-2141

9.38e-52

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

Pssm-ID: 197549 Cd Length: 130 Bit Score: 179.12 E-value: 9.38e-52

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  2012 FEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 2090
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772  2091 TMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEEC 2141
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

5.59e-51

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 176.37 E-value: 5.59e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

1.42e-50

Pssm-ID: 270204 Cd Length: 117 Bit Score: 175.15 E-value: 1.42e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

2.00e-50

Pssm-ID: 269999 Cd Length: 117 Bit Score: 174.76 E-value: 2.00e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD2_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

1.43e-49

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 172.54 E-value: 1.43e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD2_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

1.94e-49

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 172.15 E-value: 1.94e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

Pro_isomerase

pfam00160

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...

3110-3255

9.83e-49

Pssm-ID: 459694 [Multi-domain] Cd Length: 149 Bit Score: 171.28 E-value: 9.83e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITkhdGTGGQSIYGDKFEDENFDVKHT-GP 3188
Cdd:pfam00160    6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPLLLKhKR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3189 GLLSMANQGQ--NTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESfGSPKGSV-CRRITITECG 3255
Cdd:pfam00160   80 GALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEK-VPTDGDRpVKPVKILSCG 148

RanBD1_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1300

1.05e-48

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

Pssm-ID: 269992 Cd Length: 117 Bit Score: 169.95 E-value: 1.05e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFdvESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13171      1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1300
Cdd:cd13171     79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKA 114

RanBD3_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

5.65e-46

Pssm-ID: 270204 Cd Length: 117 Bit Score: 162.06 E-value: 5.65e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd14685      1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd14685     81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2959-3074

5.90e-46

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

Pssm-ID: 269995 Cd Length: 118 Bit Score: 162.19 E-value: 5.90e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2959 GEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVW 3038
Cdd:cd13174      2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3039 TASDYA-DGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13174     82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118

YRB1

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

1950-2142

3.08e-45

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 163.65 E-value: 3.08e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1950 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQYGKMANKANTSGDFEK---DDDAYKTEDSDDIHFEPVVQMpEKVELVT 2026
Cdd:COG5171     10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2027 GEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMW 2106
Cdd:COG5171     85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462575772 2107 L-ASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:COG5171    165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201

RanBD2_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

3.31e-45

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

Pssm-ID: 269993 Cd Length: 118 Bit Score: 159.92 E-value: 3.31e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKT-SGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSF 1263
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKEdNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1264 VWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD2_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

4.74e-45

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 159.44 E-value: 4.74e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd13177      1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13177     81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD2_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

8.23e-45

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

Pssm-ID: 269993 Cd Length: 118 Bit Score: 158.77 E-value: 8.23e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKN-EVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAW 2104
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2105 MWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD2_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

1.09e-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 insects and nematodes. RanBD repeat 2 is present in this hierarchy.

Pssm-ID: 269993 Cd Length: 118 Bit Score: 158.38 E-value: 1.09e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWH-TMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNAL 3036
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 3037 VWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD2_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 2; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

4.28e-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 insects and nematodes. RanBD repeat 2 is present in this hierarchy.

Pssm-ID: 269993 Cd Length: 118 Bit Score: 156.84 E-value: 4.28e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVW 2401
Cdd:cd13172      1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2402 LWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13172     81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD4_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

9.09e-44

Pssm-ID: 269999 Cd Length: 117 Bit Score: 155.88 E-value: 9.09e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13178      1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13178     81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

YRB1

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

2882-3082

1.16e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 159.41 E-value: 1.16e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2882 SFADLASSNSGDfAFGSKDKNFQWANTGAAVFGTQsvgtqsagKVGEDEDGSDEEvvhNEDIHFEPIVSLPEVEVKSGEE 2961
Cdd:COG5171     20 KERSLDVVSKGD-AFGDGKAGGEEKKVQQSPFLEN--------AVPEGDEGKGPE---SPNIHFEPVVELQRVHLKTNEE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2962 DEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWT-A 3040
Cdd:COG5171     88 DETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsT 167

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462575772 3041 SDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQK 3082
Cdd:COG5171    168 ADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALK 209

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3074

1.46e-43

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 155.19 E-value: 1.46e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

YRB1

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

1170-1303

2.30e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 158.26 E-value: 2.30e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1170 HFEPVVPLpDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISP 1249
Cdd:COG5171     70 HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINP 148

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 1250 DMKLTPNAGSDRSFVWH-ALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1303
Cdd:COG5171    149 EFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEH 203

RanBD4_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1301

5.94e-43

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

Pssm-ID: 269995 Cd Length: 118 Bit Score: 153.72 E-value: 5.94e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1265 WHALDYA-DELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13174     81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118

RanBD3_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

1.03e-42

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

Pssm-ID: 269994 Cd Length: 115 Bit Score: 152.64 E-value: 1.03e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQnmKGTERVWL 2402
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAK 113

RanBD1_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2140

2.32e-42

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

Pssm-ID: 269992 Cd Length: 117 Bit Score: 151.85 E-value: 2.32e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEvsQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYVDK--EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2140
Cdd:cd13171     79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTK 113

cyclophilin_RING

cd01923

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...

3110-3242

1.27e-41

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.

Pssm-ID: 238904 [Multi-domain] Cd Length: 159 Bit Score: 151.41 E-value: 1.27e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3188
Cdd:cd01923      8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462575772 3189 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPK 3242
Cdd:cd01923     84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPG 137

cyclophilin_SpCYP2_like

cd01922

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...

3110-3235

1.37e-41

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.

Pssm-ID: 238903 [Multi-domain] Cd Length: 146 Bit Score: 150.76 E-value: 1.37e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3188
Cdd:cd01922      6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2462575772 3189 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKI 3235
Cdd:cd01922     82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM 128

RanBD3_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

1185-1302

1.62e-41

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

Pssm-ID: 269994 Cd Length: 115 Bit Score: 149.17 E-value: 1.62e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDveSKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNagSDRSFV 1264
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFV--DKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKK--DEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1265 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQS 1302
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKN 114

RanBD1_RanBP2-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

1.12e-40

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 147.10 E-value: 1.12e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2402
Cdd:cd14684      1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2403 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd14684     81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD4_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2142

1.66e-40

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

Pssm-ID: 269995 Cd Length: 118 Bit Score: 146.40 E-value: 1.66e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13174      1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2106 WLASDFS-DGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13174     81 WGGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118

RanBD3_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2026-2140

1.90e-40

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

Pssm-ID: 269994 Cd Length: 115 Bit Score: 146.09 E-value: 1.90e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAevSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPlsGSDRAWM 2105
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462575772 2106 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2140
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111

PpiB

COG0652

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...

3094-3237

2.88e-40

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

Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 147.62 E-value: 2.88e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3094 ETNPVVFFDVcadgePLGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQsiyG 3173
Cdd:COG0652      4 APNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---G 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 3174 DKFEDENF-DVKHTgPGLLSMAN-QGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIES 3237
Cdd:COG0652     72 YTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136

RanBD1_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2323-2439

4.53e-40

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

Pssm-ID: 269992 Cd Length: 117 Bit Score: 145.30 E-value: 4.53e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVW 2401
Cdd:cd13171      1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 2402 LWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13171     78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115

Cyclophilin_PPIL3_like

cd01928

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...

3110-3244

2.79e-39

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.

Pssm-ID: 238909 [Multi-domain] Cd Length: 153 Bit Score: 144.50 E-value: 2.79e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTGekGFgFKNSIFHRVIPDFVCQGGDITkHDGTGGQSIYGDKFEDENFD-VKHTGP 3188
Cdd:cd01928      9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREtLKHDSR 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 3189 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGS 3244
Cdd:cd01928     85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKY 140

RanBD1_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 1; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3075

5.27e-39

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

Pssm-ID: 269992 Cd Length: 117 Bit Score: 142.22 E-value: 5.27e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWdrdVS-QWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNAL 3036
Cdd:cd13171      1 TGEENEEVLFCARAKLFRY---VDkEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 3037 VWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQ 3075
Cdd:cd13171     78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKK 116

YRB1

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

2282-2444

5.85e-39

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 145.93 E-value: 5.85e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2282 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN 2361
Cdd:COG5171     44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2362 YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 2440
Cdd:COG5171    123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                   ....
gi 2462575772 2441 AQEK 2444
Cdd:COG5171    203 HNEK 206

cyclophilin_WD40

cd01927

cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...

3110-3243

6.50e-38

cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known.

Pssm-ID: 238908 [Multi-domain] Cd Length: 148 Bit Score: 140.29 E-value: 6.50e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFralCTGEKGFGFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3188
Cdd:cd01927      6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRP 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 3189 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3243
Cdd:cd01927     82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKN 136

RanBD4_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 4; RanBP2 (also called E3 SUMO-protein ligase ...

2324-2438

8.77e-36

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

Pssm-ID: 269995 Cd Length: 118 Bit Score: 132.92 E-value: 8.77e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2324 GEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLW 2403
Cdd:cd13174      2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462575772 2404 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 2438
Cdd:cd13174     82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQC 117

RanBD3_RanBP2_insect-like

Ran-binding protein 2, Ran binding domain repeat 3; RanBP2 (also called E3 SUMO-protein ligase ...

2958-3076

4.56e-35

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

Pssm-ID: 269994 Cd Length: 115 Bit Score: 131.07 E-value: 4.56e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRdvSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNvsNNALV 3037
Cdd:cd13173      1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKD--EKSWM 76

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 3038 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3076
Cdd:cd13173     77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115

cyclophilin_CeCYP16-like

cd01925

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...

3110-3225

6.29e-31

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.

Pssm-ID: 238906 [Multi-domain] Cd Length: 171 Bit Score: 121.30 E-value: 6.29e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3188
Cdd:cd01925     14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 3189 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFV 3225
Cdd:cd01925     90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126

IR1-M

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2734-2790

4.51e-28

Pssm-ID: 463488 Cd Length: 60 Bit Score: 108.71 E-value: 4.51e-28

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575772 2734 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQY 2790
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLY 56

cyclophilin_RRM

cd01921

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...

3110-3252

1.09e-23

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.

Pssm-ID: 238902 [Multi-domain] Cd Length: 166 Bit Score: 100.11 E-value: 1.09e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCTgEKGFGFknSIFHRVIPDFVCQGGDITkHDGTGGQSIYGDK-------FEDE-NF 3181
Cdd:cd01921      6 LGDLVIDLFTDECPLACLNFLKLCK-LKYYNF--CLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfFEPEiLP 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462575772 3182 DVKHTGPGLLSMANQGQNTNNSQFVITLKKA-EHLDFKHVVFGFVKDGMDTVKKI-ESFGSPKGSVCRRITIT 3252
Cdd:cd01921     82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIK 154

PTZ00221

cyclophilin; Provisional

3099-3255

2.22e-22

cyclophilin; Provisional

Pssm-ID: 140248 Cd Length: 249 Bit Score: 99.17 E-value: 2.22e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3099 VFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGF----GFKNSIFHRVIPDFVCQGGDITKHD-GTGGQSIYG 3173
Cdd:PTZ00221    55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdtntGVKLDYLYTPVHHVDRNNNIIVLGElDSFNVSSTG 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3174 DKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFgsPKGSVCR---RIT 3250
Cdd:PTZ00221   135 TPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL--PLDDVGRpllPVT 212


                   ....*
gi 2462575772 3251 ITECG 3255
Cdd:PTZ00221   213 VSFCG 217

RanBD_NUP50

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...

1185-1301

4.55e-22

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha:importin-beta heterodimer, which allows for transportation of many nuclear-targeted proteins through nuclear pore complexes. It is thought to function primarily at the terminal stages of nuclear protein import to coordinate import complex disassembly and importin recycling. NUP50 is composed of a N-terminal NUP50 domain which binds the C-terminus of importin-beta, a central domain which binds importin-beta, and a C-terminal RanBD which binds importin-beta through Ran-GTP. NUP50:importin-alpha then binds cargo and can stimulate nuclear import. The N-terminal domain of NUP50 is also able to displace nuclear localization signals from importin-alpha. NUP50 interacts with cyclin-dependent kinase inhibitor 1B which binds to cyclin E-CDK2 or cyclin D-CDK4 complexes and prevents its activation, thereby controling the cell cycle progression at G1. Fungal Nup2 transiently associates with nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.

Pssm-ID: 269991 Cd Length: 111 Bit Score: 93.44 E-value: 4.55e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDvESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1264
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVG 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 1265 WHALDyadelPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13170     80 CVPNP-----GKPVTYLLRVKTAEDADELAKALEEEK 111

RanBD_NUP50

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...

2026-2142

3.40e-19

Pssm-ID: 269991 Cd Length: 111 Bit Score: 85.35 E-value: 3.40e-19

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDaEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDrawm 2105
Cdd:cd13170      1 AGEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2462575772 2106 wLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13170     76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111

cyclophilin_EcCYP_like

cd01920

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...

3110-3237

1.54e-17

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.

Pssm-ID: 238901 [Multi-domain] Cd Length: 155 Bit Score: 82.11 E-value: 1.54e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3110 LGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHdgtGGQSIYGDKFEDENFDVKHTGPG 3189
Cdd:cd01920      6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEAGNGLSNTRG 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462575772 3190 LLSMA-NQGQNTNNSQFVITLKKAEHLDFK-----HVVFGFVKDGMDTVKKIES 3237
Cdd:cd01920     80 TIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAG 133

RanBD_NUP50_plant

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...

2323-2439

9.08e-17

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

Pssm-ID: 269990 Cd Length: 117 Bit Score: 78.65 E-value: 9.08e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWl 2402
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTF- 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 2403 wtAC--DFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13169     78 --ACvnSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114

RanBD_NUP2

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...

2026-2142

1.81e-16

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore complexes (NPCs) and when artificially tethered to DNA, can prevent the spread of transcriptional activation or repression between flanking genes, a function termed boundary activity (BA). Nup2 and the Ran guanylyl-nucleotide exchange factor, Prp20, interact at specific chromatin regions and enable the NPC to play an active role in chromatin organization. Nup60p, the nup responsible for anchoring Nup2 and the Mlp proteins to the NPC is required for Nup2-dependent BA. Nup2 contains an N-terminal Nup50 family domain and a C-terminal RanBD. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.

Pssm-ID: 270002 Cd Length: 115 Bit Score: 77.86 E-value: 1.81e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQ--WKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPL-SGSDR 2102
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMgNGSLV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 2462575772 2103 AWMWLasdfsDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2142
Cdd:cd13181     81 RVPTI-----NSDGKIETYVIKVKTAADGEELLKALNDAK 115

LapB

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...

32-221

4.50e-16

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

Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 81.31 E-value: 4.50e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   32 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 111
Cdd:COG2956     83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  112 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 191
Cdd:COG2956    162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                          170       180       190
                   ....*....|....*....|....*....|
gi 2462575772  192 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 221
Cdd:COG2956    240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

RanBD_RanBP3

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...

2323-2434

4.77e-16

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike the related proteins RanBP1 and RanBP2, which promote disassembly of the export complex in the cytosol, acts as a CRM1 cofactor, enhancing nuclear export signal (NES) export by stabilizing the export complex in the nucleus. CRM1/Exportin1 is responsible for exporting many proteins and ribonucleoproteins from the nucleus to the cytosol. RanBP3 also alters the cargo selectivity of CRM1, promoting recognition of the NES of HIV-1 Rev and of other cargos while deterring recognition of the import adaptor protein Snurportin1. RanBP3 contains a N-terminal nuclear localization signal (NLS), 2 FxFG motifs, and a single RanBD. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity.

Pssm-ID: 270001 Cd Length: 113 Bit Score: 76.50 E-value: 4.77e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKI--LQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQnmKGTERV 2400
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVE--KVSEKS 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462575772 2401 WLWTAcdfADGERKVEHLAVRFKLQDVADSFKKI 2434
Cdd:cd13180     79 LRITA---MDDEGQVKVFLLQASPEDAKQLYNAI 109

RanBD_NUP50

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...

2324-2439

6.52e-16

Pssm-ID: 269991 Cd Length: 111 Bit Score: 76.10 E-value: 6.52e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2324 GEENEQVVFSHRAKLYRYDKDvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTlqnMKGTERVWLW 2403
Cdd:cd13170      2 GEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMP---YSVAGKNNVF 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462575772 2404 TACDFADGerKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13170     78 VGCVPNPG--KPVTYLLRVKTAEDADELAKALEEEK 111

RanBD_RanBP3

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...

2026-2098

2.07e-15

Pssm-ID: 270001 Cd Length: 113 Bit Score: 74.58 E-value: 2.07e-15

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKL--RMLMRREQVLKVCANHWITTTMNLKPLS 2098
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGqsRIVMRTQGSLRVILNTKIWPGMTVEKVS 75

IR1-M

Nup358/RanBP2 E3 ligase domain; This domain family is found in eukaryotes, and is ...

2656-2718

3.03e-15

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 3.03e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462575772 2656 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2718
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

RanBD_NUP2

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...

1185-1301

7.25e-15

Pssm-ID: 270002 Cd Length: 115 Bit Score: 73.24 E-value: 7.25e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKE--WKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPnAGSDRS 1262
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEK-MGNGSL 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 1263 FVWHALDYADELpkpEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13181     80 VRVPTINSDGKI---ETYVIKVKTAADGEELLKALNDAK 115

RanBD_NUP50_plant

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...

2026-2140

7.53e-15

Pssm-ID: 269990 Cd Length: 117 Bit Score: 73.25 E-value: 7.53e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2026 TGEEDEKVLYSQRVKLFRFDAevSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2105
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462575772 2106 WLASdFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2140
Cdd:cd13169     79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112

LapB

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...

28-287

6.46e-14

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

Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 74.77 E-value: 6.46e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   28 GFYF-AKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELL 103
Cdd:COG2956     10 GWYFkGLNYLLNGQPDKAIDL---LEEALELDPEtveAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  104 CKNDVTDgRAKYWLERAAKLFPGSPAIYklkEQLLDC---EGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRL 180
Cdd:COG2956     87 LKAGLLD-RAEELLEKLLELDPDDAEAL---RLLAEIyeqEGD--WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  181 KDAVAHCHEA-------ERNIALRSSLEWNscvvqtLKEYLESLQCLEsdksDWRATNTDLLLAYANLMLLTLSTRDVQE 253
Cdd:COG2956    161 DEAIEALEKAlkldpdcARALLLLAELYLE------QGDYEEAIAALE----RALEQDPDYLPALPRLAELYEKLGDPEE 230

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2462575772  254 SRELLQsfdSALQSVKSLGGNDELSATFLEMKGH 287
Cdd:COG2956    231 ALELLR---KALELDPSDDLLLALADLLERKEGL 261

RanBD_RanBP3

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...

1185-1262

6.70e-14

Pssm-ID: 270001 Cd Length: 113 Bit Score: 70.34 E-value: 6.70e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKI--LRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPnaGSDRS 1262
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEK--VSEKS 78

RanBD_NUP50

Nucleoporin 50 Ran-binding domain; NUP50 acts as a cofactor for the importin-alpha: ...

2959-3074

8.99e-14

Pssm-ID: 269991 Cd Length: 111 Bit Score: 69.94 E-value: 8.99e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2959 GEEDEEILFKERAKLYRWDrDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVW 3038
Cdd:cd13170      2 GEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVGC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462575772 3039 TASDyadgeAKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13170     81 VPNP-----GKPVTYLLRVKTAEDADELAKALEEEK 111

RanBD_NUP50_plant

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...

1185-1300

1.93e-13

Pssm-ID: 269990 Cd Length: 117 Bit Score: 69.40 E-value: 1.93e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1185 TGEEDEEEFFCNRAKLFRFDveSKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSF- 1263
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFI--DGGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFa 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1264 -VWHAldyADELPKPEQLAIRFKTPEEAALFKCKFEEA 1300
Cdd:cd13169     79 cVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAH 113

RanBD_NUP2

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...

2958-3074

7.75e-13

Pssm-ID: 270002 Cd Length: 115 Bit Score: 67.46 E-value: 7.75e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWD--RDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNvsNNA 3035
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMG--NGS 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 3036 LVWTASDYADGeaKVEQLAVRFKTKEVADCFKKTFEECQ 3074
Cdd:cd13181     79 LVRVPTINSDG--KIETYVIKVKTAADGEELLKALNDAK 115

RanBD_RanBP3

Ran-binding protein 3 Ran-binding domain; RanBP3, a Ran-interacting nuclear protein, unlike ...

2958-3068

1.26e-12

Pssm-ID: 270001 Cd Length: 113 Bit Score: 66.87 E-value: 1.26e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKI--LWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPlnVSNNA 3035
Cdd:cd13180      1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEK--VSEKS 78

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2462575772 3036 LVWTASDyADGEAKVeqLAVRFKTKEVADCFKK 3068
Cdd:cd13180     79 LRITAMD-DEGQVKV--FLLQASPEDAKQLYNA 108

RanBD_NUP2

Nucleoporin 2 Ran-binding domain; Yeast protein Nup2 transiently associates with Nuclear pore ...

2323-2439

9.22e-12

Pssm-ID: 270002 Cd Length: 115 Bit Score: 64.38 E-value: 9.22e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2323 SGEENEQVVFSHRAKLYRYD--KDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMkGTERV 2400
Cdd:cd13181      1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKM-GNGSL 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462575772 2401 WLWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2439
Cdd:cd13181     80 VRVPT---INSDGKIETYVIKVKTAADGEELLKALNDAK 115

zf-RanBP

Zn-finger in Ran binding protein and others;

1780-1808

6.59e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.59e-11

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1780 RKGQWDCSVCCVQNESSSLKCVACDASKP 1808
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

BepA

COG4783

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...

29-138

6.63e-11

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 62.52 E-value: 6.63e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDV 108
Cdd:COG4783      8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGD 87

                           90       100       110
                   ....*....|....*....|....*....|
gi 2462575772  109 TDGRAKYWlERAAKLFPGSPAIYKLKEQLL 138
Cdd:COG4783     88 YDEALALL-EKALKLDPEHPEAYLRLARAY 116

TPR

COG0457

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

29-259

1.15e-10

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

Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 64.64 E-value: 1.15e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYictY---INVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK 105
Cdd:COG0457     12 NNLGLAYRRLGRYEEAIED---YekaLELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  106 ndvtDGR---AKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKD 182
Cdd:COG0457     89 ----LGRyeeALEDYDKALELDPDDAEALYNLGLALLELGR--YDEAIEAYERALELDPDDADALYNLGIALEKLGRYEE 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462575772  183 AVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQ 259
Cdd:COG0457    163 ALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239

zf-RanBP

Zn-finger in Ran binding protein and others;

1478-1507

1.34e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.34e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1478 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1507
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1664-1693

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1664 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1693
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1605-1634

1.86e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.86e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1605 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1634
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

PRK10903

peptidylprolyl isomerase A;

3111-3235

3.37e-10

peptidylprolyl isomerase A;

Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 62.17 E-value: 3.37e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3111 GRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHdgtGGQSIYGDKFEDENFDVKHTGPGL 3190
Cdd:PRK10903    38 GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFTEQ---MQQKKPNPPIKNEADNGLRNTRGT 111

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462575772 3191 LSMANQG-QNTNNSQFVITLKKAEHL-----DFKHVVFGFVKDGMDTVKKI 3235
Cdd:PRK10903   112 IAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKI 162

zf-RanBP

Zn-finger in Ran binding protein and others;

1542-1571

5.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1542 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1571
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1723-1752

1.26e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.26e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 2462575772 1723 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1752
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

PRK10791

peptidylprolyl isomerase B;

3111-3237

1.82e-08

peptidylprolyl isomerase B;

Pssm-ID: 182734 Cd Length: 164 Bit Score: 56.39 E-value: 1.82e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3111 GRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhdGTGGQSIYGDKFEDENFDVKHTgPGL 3190
Cdd:PRK10791     9 GDIVIKTFDDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGFEP--GMKQKATKEPIKNEANNGLKNT-RGT 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462575772 3191 LSMA-NQGQNTNNSQFVITLKKAEHLDFK--------HVVFGFVKDGMDTVKKIES 3237
Cdd:PRK10791    83 LAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKG 138

PH-like

cd00900

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...

1194-1297

2.72e-08

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.

Pssm-ID: 275390 Cd Length: 89 Bit Score: 53.56 E-value: 2.72e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1194 FCNRAKLFRFdveskEWKERGIGNVKILrhktsgKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRS--FVWHALDya 1271
Cdd:cd00900      1 LKFRAVRVYR-----EPTKRVEGTLYIT------SDRLILRDKNDGGLELSIPISDIVNVNVSPQGPSSryLVLVLKD-- 67

                           90       100
                   ....*....|....*....|....*.
gi 2462575772 1272 delpKPEQLAIRFKTPEEAALFKCKF 1297
Cdd:cd00900     68 ----RGEFVGFSFPKEEDAIEISDAL 89

zf-RanBP

Zn-finger in Ran binding protein and others;

1414-1442

3.08e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.08e-08

                           10        20
                   ....*....|....*....|....*....
gi 2462575772 1414 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1442
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

TPR

COG0457

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

52-297

5.50e-08

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

Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 56.55 E-value: 5.50e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   52 INVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAIY 131
Cdd:COG0457      1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE-EALADYEQALELDPDDAEAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  132 KLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEA-ERNIALRSSLEWNSCVVQTL 210
Cdd:COG0457     80 NNLGLALQALGR--YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAlELDPDDADALYNLGIALEKL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  211 KEYLESLQCLEsdKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYM 290
Cdd:COG0457    158 GRYEEALELLE--KLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRL 235


                   ....*..
gi 2462575772  291 HAGSLLL 297
Cdd:COG0457    236 AALALYQ 242

TadD

COG5010

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...

34-125

5.88e-08

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];

Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 54.58 E-value: 5.88e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   34 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 113
Cdd:COG5010     63 LYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDD-EA 141

                           90
                   ....*....|..
gi 2462575772  114 KYWLERAAKLFP 125
Cdd:COG5010    142 KAALQRALGTSP 153

NrfG

COG4235

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...

58-131

9.42e-08

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 53.47 E-value: 9.42e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575772   58 DPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAIY 131
Cdd:COG4235     16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE-EAEELLERALALDPDNPEAL 88

PilF

COG3063

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

34-125

7.30e-07

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

Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 49.78 E-value: 7.30e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   34 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVEcYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 113
Cdd:COG3063      1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD-EA 78

                           90
                   ....*....|..
gi 2462575772  114 KYWLERAAKLFP 125
Cdd:COG3063     79 LAYLERALELDP 90

cyclophilin_TLP40_like

cd01924

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...

3111-3236

7.55e-07

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.

Pssm-ID: 238905 Cd Length: 176 Bit Score: 52.06 E-value: 7.55e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3111 GRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHD------GTG--------------GQS 3170
Cdd:cd01924      7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 3171 IYGDKFE-----DENFDVKHTGPGLLSMANQ--GQNTNNSQFVITLKKAEH-------LDFKHVVFGFVKDGMDTVKKIE 3236
Cdd:cd01924     84 VYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLDILRELK 163

zf-RanBP

Zn-finger in Ran binding protein and others;

1350-1380

7.87e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.87e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 2462575772 1350 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1380
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKPD 30

CpoB

COG1729

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...

33-137

1.11e-06

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

Pssm-ID: 441335 [Multi-domain] Cd Length: 113 Bit Score: 49.60 E-value: 1.11e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   33 KLYYEAKEYDLAKKYictYINVQERDPK------AHRFLGLLYELEENTDKAVECYRRSVELNPTQK---DLVLKIAELL 103
Cdd:COG1729      1 KALLKAGDYDEAIAA---FKAFLKRYPNsplapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSY 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462575772  104 CKNDVTDgRAKYWLERAAKLFPGSPAIYKLKEQL 137
Cdd:COG1729     78 LELGDYD-KARATLEELIKKYPDSEAAKEARARL 110

RanBD_NUP50_plant

Ran-binding protein 2, repeat 1; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa ...

2958-3072

2.03e-06

Pssm-ID: 269990 Cd Length: 117 Bit Score: 48.98 E-value: 2.03e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 2958 SGEEDEEILFKERAKLYRWDRdvSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3037
Cdd:cd13169      1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2462575772 3038 WTASdYADGEAKVEQLAVRFKTKEVADCFKKTFEE 3072
Cdd:cd13169     79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112

BepA

COG4783

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...

30-125

3.74e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 49.03 E-value: 3.74e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   30 YFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVT 109
Cdd:COG4783     43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                           90
                   ....*....|....*.
gi 2462575772  110 DGRAKYWlERAAKLFP 125
Cdd:COG4783    123 DEAIAAL-EKALELDP 137

ZnF_RBZ

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

1666-1690

6.81e-06

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 45.00 E-value: 6.81e-06

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1666 GQWDCSVCLVRNEASATKCIACQNP 1690
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1607-1631

6.81e-06

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 45.00 E-value: 6.81e-06

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1607 GQWDCSVCLVRNEASATKCIACQNP 1631
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

BepA

COG4783

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...

29-92

1.01e-05

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 47.88 E-value: 1.01e-05

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQ 92
Cdd:COG4783     76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139

ZnF_RBZ

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

1725-1747

5.17e-05

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 42.30 E-value: 5.17e-05

                            10        20
                    ....*....|....*....|...
gi 2462575772  1725 GQWDCSVCLVRNEASATKCIACQ 1747
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23

ZnF_RBZ

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

1782-1806

7.51e-05

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.92 E-value: 7.51e-05

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1782 GQWDCSVCCVQNESSSLKCVACDAS 1806
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TadD

COG5010

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...

32-90

1.20e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];

Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 44.95 E-value: 1.20e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462575772   32 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 90
Cdd:COG5010     95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153

ZnF_RBZ

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

1480-1504

1.35e-04

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 1.35e-04

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1480 GQWDCSACLVQNEGSSTKCAACQNP 1504
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR

smart00028

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...

59-91

1.37e-04

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.

Pssm-ID: 197478 [Multi-domain] Cd Length: 34 Bit Score: 41.28 E-value: 1.37e-04

                            10        20        30
                    ....*....|....*....|....*....|...
gi 2462575772    59 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 91
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33

Spy

COG3914

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...

31-266

1.43e-04

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

Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 47.68 E-value: 1.43e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   31 FAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK-NDVT 109
Cdd:COG3914     84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRlGRLE 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  110 DGRAKYwlERAAKLFPGSPAIYklkeqlldcegedgwnklfdliqselyvrpddvhvnIRLVEVYRSTKRLKDAVAHCHE 189
Cdd:COG3914    164 EAIAAL--RRALELDPDNAEAL------------------------------------NNLGNALQDLGRLEEAIAAYRR 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  190 AER----NIALRSSLE---WNSCVVQTLKEYLESLQCLESDKSDWratntdlllayANLMLLTLSTRDVQESRELLQSFD 262
Cdd:COG3914    206 ALEldpdNADAHSNLLfalRQACDWEVYDRFEELLAALARGPSEL-----------SPFALLYLPDDDPAELLALARAWA 274


                   ....
gi 2462575772  263 SALQ 266
Cdd:COG3914    275 QLVA 278

Spy

COG3914

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...

29-131

1.44e-04

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

Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 47.68 E-value: 1.44e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK-ND 107
Cdd:COG3914    116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDlGR 195

                           90       100
                   ....*....|....*....|....
gi 2462575772  108 VTDGRAkyWLERAAKLFPGSPAIY 131
Cdd:COG3914    196 LEEAIA--AYRRALELDPDNADAH 217

ZnF_RBZ

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

1544-1568

1.51e-04

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

Pssm-ID: 197784 [Multi-domain] Cd Length: 25 Bit Score: 41.15 E-value: 1.51e-04

                            10        20
                    ....*....|....*....|....*
gi 2462575772  1544 GQWDCSSCLVRNEANATRCVACQNP 1568
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR_1

pfam00515

Tetratricopeptide repeat;

59-91

1.76e-04

Tetratricopeptide repeat;

Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 40.87 E-value: 1.76e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462575772   59 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 91
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33

PEP_TPR_lipo

TIGR02917

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...

29-290

1.93e-04

Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.39 E-value: 1.93e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAE-LLC 104
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  105 KNDVtdGRAKYWLERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVEVYRSTKRLKd 182
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772  183 avahchEAERniALRSSLEWnscvvqtlkeyleslqclesdKSDwratNTDLLLAYANLMLLTlstrdvqesrellQSFD 262
Cdd:TIGR02917  653 ------KAIT--SLKRALEL---------------------KPD----NTEAQIGLAQLLLAA-------------KRTE 686

                          250       260
                   ....*....|....*....|....*...
gi 2462575772  263 SALQSVKSLGGNDELSATFLEMKGHFYM 290
Cdd:TIGR02917  687 SAKKIAKSLQKQHPKAALGFELEGDLYL 714

NrfG

COG4235

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...

29-90

3.47e-04

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 43.07 E-value: 3.47e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462575772   29 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 90
Cdd:COG4235     55 LDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLP 116

RanBD5_RanBP2_insect-like

cd13175

Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase ...

1187-1301

4.34e-04

Ran-binding protein 2, Ran binding domain repeat 5; RanBP2 (also called E3 SUMO-protein ligase RanBP2, 358 kDa nucleoporin, and nuclear pore complex (NPC) protein Nup358) is a giant nucleoporin that localizes to the cytosolic face of the NPC. RanBP2 contains a leucine-rich region, 8 zinc-finger motifs, a cyclophilin A homologous domain, and 4 RanBDs. Ran is a Ras-like nuclear small GTPase, which regulates receptor-mediated transport between the nucleus and the cytoplasm. RanGTP hydrolysis is stimulated by RanGAP together with the Ran-binding domain containing acessory proteins RanBP1 and RanBP2. These accessory proteins stabilize the active GTP-bound form of Ran. All eukaryotic cells contain RanBP1, but in vertebrates however, the main RanBP seems to be RanBP2. There is no RanBP2 ortholog in yeast. Transport complex disassembly is accomplished by a small ubiquitin-related modifier-1 (SUMO-1)-modified version of RanGAP that is bound to RanBP2. RanBP1 acts as a second line of defense against exported RanGTP-importin complexes which have escaped from dissociation by RanBP2. RanBP2 also interacts with the importin subunit beta-1. RabBD shares structural similarity to the PH domain, but lacks detectable sequence similarity. The members here include insects and nematodes. RanBD repeat 5 is present in this hierarchy.

Pssm-ID: 269996 Cd Length: 114 Bit Score: 42.52 E-value: 4.34e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772 1187 EEDEEEF-FCNRAKLFRFDVESKEWKERGIGNVKILRHKT--SGKIRLLMRREQVlkICANHYISPDMKLTPnagSDRSF 1263
Cdd:cd13175      2 DDDEELFmFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEiyGARIVLSDDDTDT--IIANTIIAVQTSLRV---EGKEA 76

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462575772 1264 VWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1301
Cdd:cd13175     77 IWSAIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK 114

TPR_2

pfam07719

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...

59-91

6.37e-04

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.

Pssm-ID: 429619 [Multi-domain] Cd Length: 33 Bit Score: 39.43 E-value: 6.37e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462575772   59 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 91
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33

NlpI

COG4785

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];

34-128

6.98e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 443815 [Multi-domain] Cd Length: 223 Bit Score: 43.75 E-value: 6.98e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   34 LYYEAKEYDLAkkyICTYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLK--IAELLckndv 108
Cdd:COG4785     82 AYDSLGDYDLA---IADFDQALELDPDlaeAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNrgIALYY----- 153

                           90       100
                   ....*....|....*....|...
gi 2462575772  109 tDGR---AKYWLERAAKLFPGSP 128
Cdd:COG4785    154 -LGRyelAIADLEKALELDPNDP 175

TadD

COG5010

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...

51-138

9.29e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];

Pssm-ID: 444034 [Multi-domain] Cd Length: 155 Bit Score: 42.64 E-value: 9.29e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462575772   51 YINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAI 130
Cdd:COG5010     46 GRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKD-EAKEYYEKALALSPDNPNA 124


                   ....*...
gi 2462575772  131 YKLKEQLL 138
Cdd:COG5010    125 YSNLAALL 132

ZnF_RBZ