NCBI Conserved Domain Search

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

2027-2143

1.09e-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: 1.09e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

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

1186-1302

3.35e-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: 3.35e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

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

2324-2440

1.62e-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: 1.62e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd14685    81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

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

2925-3041

2.18e-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: 2.18e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

IR1-M

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

2709-2769

1.13e-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: 110.64 E-value: 1.13e-28

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150418007  2709 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQKSQTE 2769
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLYPDDE 60

LapB

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

33-222

4.45e-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: 4.45e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  113 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 150418007  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

IR1-M super family

cl13601

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

2631-2693

2.77e-15

The actual alignment was detected with superfamily member pfam12185:

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 2.77e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150418007  2631 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2693
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

zf-RanBP

Zn-finger in Ran binding protein and others;

1781-1809

6.52e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.52e-11

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1781 RKGQWDCSVCCVQNESSSLKCVACDASKP 1809
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1479-1508

1.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1479 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1508
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1606-1635

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1606 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1635
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1665-1694

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1665 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1694
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1543-1572

5.28e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.28e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1543 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1572
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1724-1753

1.25e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.25e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1724 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1753
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1415-1443

3.05e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.05e-08

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1415 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1443
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1351-1381

7.79e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.79e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 150418007  1351 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1381
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 ...

3064-3222

3.59e-94

Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 301.87 E-value: 3.59e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3064 PVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKG-----FGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSI 3138
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3139 YGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITI 3218
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 150418007 3219 TECG 3222
Cdd:cd01926   161 ADCG 164

RanBD2_RanBP2-like

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

2027-2143

1.09e-83

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 269.99 E-value: 1.09e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

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

1186-1302

3.35e-83

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 268.44 E-value: 3.35e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

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

2324-2440

1.62e-82

Pssm-ID: 270204 Cd Length: 117 Bit Score: 266.83 E-value: 1.62e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd14685    81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

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

2925-3041

2.18e-82

Pssm-ID: 269999 Cd Length: 117 Bit Score: 266.43 E-value: 2.18e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

PTZ00060

cyclophilin; Provisional

3057-3224

8.11e-72

cyclophilin; Provisional

Pssm-ID: 240249 Cd Length: 183 Bit Score: 238.98 E-value: 8.11e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3057 ELSKetNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE------KGFGFKNSIFHRVIPDFVCQGGDITKH 3130
Cdd:PTZ00060   11 EMSK--RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3131 DGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3210
Cdd:PTZ00060   89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG 168

                         170
                  ....*....|....
gi 150418007 3211 SVCRRITITECGQI 3224
Cdd:PTZ00060  169 YPKKPVVVTDCGEL 182

Ran_BP1

RanBP1 domain;

2922-3043

3.49e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.77 E-value: 3.49e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2922 EVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNN 3001
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  3002 ALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3043
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

1183-1304

5.35e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.39 E-value: 5.35e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  1183 EVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDR 1262
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  1263 SFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1304
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

2024-2145

8.89e-67

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 221.92 E-value: 8.89e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2024 ELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 2103
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  2104 AWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRL 2145
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

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

2912-3040

1.80e-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: 1.80e-66

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2912 FEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMK-NYYRILMRRDQVFKVCANHVITKT 2990
Cdd:smart00160    1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFKS 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 150418007   2991 MELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC 3040
Cdd:smart00160   81 MTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD

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

2310-2439

2.30e-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: 218.03 E-value: 2.30e-65

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2310 FEPVVPLPDlVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 2388
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   2389 DMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 2439
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Ran_BP1

RanBP1 domain;

2321-2442

2.35e-65

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 217.68 E-value: 2.35e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2321 EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER 2400
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  2401 VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 2442
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

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

1172-1301

2.54e-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: 2.54e-54

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   1172 FEPVVPLPDkIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHK-TSGKIRLLMRREQVLKICANHYISP 1250
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   1251 DMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1301
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD

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

2013-2142

7.64e-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: 179.51 E-value: 7.64e-52

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2013 FEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 2091
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   2092 TMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEEC 2142
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Pro_isomerase

pfam00160

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

3077-3222

9.73e-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: 9.73e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  3077 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITkhdGTGGQSIYGDKFEDENFDVKHT-GP 3155
Cdd:pfam00160    6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPLLLKhKR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  3156 GLLSMANQGQ--NTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESfGSPKGSV-CRRITITECG 3222
Cdd:pfam00160   80 GALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEK-VPTDGDRpVKPVKILSCG 148

YRB1

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

1951-2143

2.61e-45

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 164.04 E-value: 2.61e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1951 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQYGKMANKANTSGDFEK---DDDAYKTEDSDDIHFEPVVQMpEKVELVT 2027
Cdd:COG5171    10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2028 GEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMW 2107
Cdd:COG5171    85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150418007 2108 L-ASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:COG5171   165 MsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQ 201

YRB1

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

2849-3049

9.56e-44

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 159.41 E-value: 9.56e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2849 SFADLASSNSGDfAFGSKDKNFQWANTGAAVFGTQsvgtqsagKVGEDEDGSDEEvvhNEDIHFEPIVSLPEVEVKSGEE 2928
Cdd:COG5171    20 KERSLDVVSKGD-AFGDGKAGGEEKKVQQSPFLEN--------AVPEGDEGKGPE---SPNIHFEPVVELQRVHLKTNEE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2929 DEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWT-A 3007
Cdd:COG5171    88 DETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsT 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 150418007 3008 SDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQK 3049
Cdd:COG5171   168 ADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALK 209

YRB1

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

1171-1304

1.92e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 158.64 E-value: 1.92e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1171 HFEPVVPLpDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISP 1250
Cdd:COG5171    70 HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINP 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150418007 1251 DMKLTPNAGSDRSFVWH-ALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1304
Cdd:COG5171   149 EFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEH 203

PpiB

COG0652

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

3061-3204

2.85e-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: 2.85e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3061 ETNPVVFFDVcadgePLGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQsiyG 3140
Cdd:COG0652     4 APNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---G 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 3141 DKFEDENF-DVKHTgPGLLSMAN-QGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIES 3204
Cdd:COG0652    72 YTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136

YRB1

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

2283-2445

4.82e-39

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 145.93 E-value: 4.82e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2283 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN 2362
Cdd:COG5171    44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2363 YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 2441
Cdd:COG5171   123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                  ....
gi 150418007 2442 AQEK 2445
Cdd:COG5171   203 HNEK 206

IR1-M

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

2709-2769

1.13e-28

Pssm-ID: 463488 Cd Length: 60 Bit Score: 110.64 E-value: 1.13e-28

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150418007  2709 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQKSQTE 2769
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLYPDDE 60

LapB

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

33-222

4.45e-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: 4.45e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  113 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 150418007  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

IR1-M

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

2631-2693

2.77e-15

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 2.77e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150418007  2631 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2693
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

zf-RanBP

Zn-finger in Ran binding protein and others;

1781-1809

6.52e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.52e-11

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1781 RKGQWDCSVCCVQNESSSLKCVACDASKP 1809
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1479-1508

1.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1479 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1508
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1606-1635

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1606 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1635
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1665-1694

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1665 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1694
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1543-1572

5.28e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.28e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1543 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1572
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1724-1753

1.25e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.25e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1724 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1753
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1415-1443

3.05e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.05e-08

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1415 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1443
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

zf-RanBP

Zn-finger in Ran binding protein and others;

1351-1381

7.79e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.79e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 150418007  1351 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1381
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKPD 30

ZnF_RBZ

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

1667-1691

6.94e-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: 6.94e-06

                            10        20
                    ....*....|....*....|....*
gi 150418007   1667 GQWDCSVCLVRNEASATKCIACQNP 1691
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1608-1632

6.94e-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: 6.94e-06

                            10        20
                    ....*....|....*....|....*
gi 150418007   1608 GQWDCSVCLVRNEASATKCIACQNP 1632
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1726-1748

5.27e-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: 5.27e-05

                            10        20
                    ....*....|....*....|...
gi 150418007   1726 GQWDCSVCLVRNEASATKCIACQ 1748
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23

ZnF_RBZ

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

1783-1807

7.58e-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: 7.58e-05

                            10        20
                    ....*....|....*....|....*
gi 150418007   1783 GQWDCSVCCVQNESSSLKCVACDAS 1807
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1481-1505

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 150418007   1481 GQWDCSACLVQNEGSSTKCAACQNP 1505
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR

smart00028

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

60-92

1.35e-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: 1.35e-04

                            10        20        30
                    ....*....|....*....|....*....|...
gi 150418007     60 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 92
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33

ZnF_RBZ

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

1545-1569

1.50e-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: 1.50e-04

                            10        20
                    ....*....|....*....|....*
gi 150418007   1545 GQWDCSSCLVRNEANATRCVACQNP 1569
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR_1

pfam00515

Tetratricopeptide repeat;

60-92

1.74e-04

Tetratricopeptide repeat;

Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 40.87 E-value: 1.74e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 150418007    60 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 92
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33

PEP_TPR_lipo

TIGR02917

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

30-291

1.91e-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: 1.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007    30 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAE-LLC 105
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   106 KNDVtdGRAKYWLERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVEVYRSTKRLKd 183
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   184 avahchEAERniALRSSLEWnscvvqtlkeyleslqclesdKSDwratNTDLLLAYANLMLLTlstrdvqesrellQSFD 263
Cdd:TIGR02917  653 ------KAIT--SLKRALEL---------------------KPD----NTEAQIGLAQLLLAA-------------KRTE 686

                          250       260
                   ....*....|....*....|....*...
gi 150418007   264 SALQSVKSLGGNDELSATFLEMKGHFYM 291
Cdd:TIGR02917  687 SAKKIAKSLQKQHPKAALGFELEGDLYL 714

ZnF_RBZ

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

1417-1440

1.11e-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: 1.11e-03

                            10        20
                    ....*....|....*....|....
gi 150418007   1417 GHWDCSICLVRNEPTVSRCIACQN 1440
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGA 24

ACL4-like

cd24142

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

33-91

6.48e-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: 6.48e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150418007   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 91
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 ...

3064-3222

3.59e-94

Pssm-ID: 238907 [Multi-domain] Cd Length: 164 Bit Score: 301.87 E-value: 3.59e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3064 PVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKG-----FGFKNSIFHRVIPDFVCQGGDITKHDGTGGQSI 3138
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3139 YGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGSVCRRITI 3218
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 150418007 3219 TECG 3222
Cdd:cd01926   161 ADCG 164

RanBD2_RanBP2-like

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

2027-2143

1.09e-83

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 269.99 E-value: 1.09e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD1_RanBP2-like

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

1186-1302

3.35e-83

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 268.44 E-value: 3.35e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

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

2324-2440

1.62e-82

Pssm-ID: 270204 Cd Length: 117 Bit Score: 266.83 E-value: 1.62e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd14685    81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

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

2925-3041

2.18e-82

Pssm-ID: 269999 Cd Length: 117 Bit Score: 266.43 E-value: 2.18e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD_RanBP2-like

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

2925-3041

5.30e-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: 5.30e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

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

1186-1302

5.68e-75

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 244.88 E-value: 5.68e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

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

2027-2143

9.80e-74

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 241.41 E-value: 9.80e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

RanBD_RanBP2-like

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

2324-2440

1.24e-72

Pssm-ID: 269997 [Multi-domain] Cd Length: 117 Bit Score: 238.33 E-value: 1.24e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd13176     1 TGEEDEEVLFSHRAKLYRFDKDVKQWKERGVGDIKILQHKTTGRIRILMRRDQVLKVCANHYITPDMKLKPNAGSDRSWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13176    81 WTALDFSEEEPKVEQLAVKFKTPEVADEFKKKFEEAQ 117

PTZ00060

cyclophilin; Provisional

3057-3224

8.11e-72

cyclophilin; Provisional

Pssm-ID: 240249 Cd Length: 183 Bit Score: 238.98 E-value: 8.11e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3057 ELSKetNPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE------KGFGFKNSIFHRVIPDFVCQGGDITKH 3130
Cdd:PTZ00060   11 EMSK--RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNH 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3131 DGTGGQSIYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3210
Cdd:PTZ00060   89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG 168

                         170
                  ....*....|....
gi 150418007 3211 SVCRRITITECGQI 3224
Cdd:PTZ00060  169 YPKKPVVVTDCGEL 182

RanBD_RanBP1

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

1170-1302

1.73e-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: 1.73e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1170 PHFEPVVPLPdKIEVKTGEEDEEEFFCNRAKLFRFD--VESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHY 1247
Cdd:cd13179     2 AQFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDteNDPPEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150418007 1248 ISPDMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13179    81 ITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

Ran_BP1

RanBP1 domain;

2922-3043

3.49e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.77 E-value: 3.49e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2922 EVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNN 3001
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  3002 ALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3043
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

1183-1304

5.35e-68

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 225.39 E-value: 5.35e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  1183 EVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDR 1262
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  1263 SFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1304
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

Ran_BP1

RanBP1 domain;

2024-2145

8.89e-67

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 221.92 E-value: 8.89e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2024 ELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDR 2103
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  2104 AWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQRL 2145
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD

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

2912-3040

1.80e-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: 1.80e-66

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2912 FEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMK-NYYRILMRRDQVFKVCANHVITKT 2990
Cdd:smart00160    1 FKPVVPLPDVEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFKS 80

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 150418007   2991 MELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEEC 3040
Cdd:smart00160   81 MTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

PLN03149

peptidyl-prolyl isomerase H (cyclophilin H); Provisional

3063-3224

6.85e-66

peptidyl-prolyl isomerase H (cyclophilin H); Provisional

Pssm-ID: 178694 Cd Length: 186 Bit Score: 222.02 E-value: 6.85e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3063 NPVVFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGE---KGF--GFKNSIFHRVIPDFVCQGGDITKHDGTGGQS 3137
Cdd:PLN03149   18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3138 IYGDKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFV-KDGMDTVKKIESFGS-----PKGS 3211
Cdd:PLN03149   98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATgpnnrPKLA 177

                         170
                  ....*....|...
gi 150418007 3212 VcrriTITECGQI 3224
Cdd:PLN03149  178 C----VISECGEM 186

RanBD

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

2310-2439

2.30e-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: 218.03 E-value: 2.30e-65

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2310 FEPVVPLPDlVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDN-KQVRIVMRRDQVLKLCANHRITP 2388
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNgGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   2389 DMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEA 2439
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

Ran_BP1

RanBP1 domain;

2321-2442

2.35e-65

RanBP1 domain;

Pssm-ID: 395513 [Multi-domain] Cd Length: 122 Bit Score: 217.68 E-value: 2.35e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  2321 EVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTER 2400
Cdd:pfam00638    1 EVKTGEEDEEVLFSQRAKLFRFDAEVKQWKERGVGDIKILKNKDDGKVRILMRRDQVLKVCANHYITPDMTLKPLAGSDR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 150418007  2401 VWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKTA 2442
Cdd:pfam00638   81 SWVWTAADFADGEGKPEQLAIRFKTKEEADSFKKKFEEAQKE 122

RanBD_RanBP1

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

2909-3042

5.88e-63

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 211.27 E-value: 5.88e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2909 DIHFEPIVSLPEVEVKSGEEDEEILFKERAKLYRWDRDVS--QWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHV 2986
Cdd:cd13179     1 DAQFEPIVKLPEVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 2987 ITKTMELKPLNVSNNALVWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQ 3042
Cdd:cd13179    81 ITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQK 136

RanBD_RanBP1

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

2010-2143

1.27e-61

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 207.42 E-value: 1.27e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2010 DIHFEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVS--QWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANH 2087
Cdd:cd13179     1 DAQFEPIVKLPE-VEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 2088 WITTTMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13179    80 YITPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

RanBD_family

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

1186-1302

4.74e-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: 4.74e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1266 WHALDYAD-ELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd00835    81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD_RanBP1

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

2309-2440

7.95e-57

Pssm-ID: 270000 [Multi-domain] Cd Length: 136 Bit Score: 193.94 E-value: 7.95e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2309 YFEPVVPLPdLVEVSSGEENEQVVFSHRAKLYRYDKDVG--QWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRI 2386
Cdd:cd13179     3 QFEPIVKLP-EVEVKTGEEDEEVLFKMRAKLYRFDTENDppEWKERGTGDVKLLKHKETKKIRLLMRRDKTLKICANHYI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150418007 2387 TPDMTLQNMKGTERVWLWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13179    82 TPEMKLKPNAGSDRAWVWTCADFADEEPKPELFAIRFANAENAQKFKEAFEEAQ 135

RanBD_family

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

2324-2440

5.06e-55

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 187.80 E-value: 5.06e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2404 WTACDFAD-GERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd00835    81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD_family

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

2027-2143

7.04e-55

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 187.42 E-value: 7.04e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2107 WLASDFSD-GDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd00835    81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD

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

1172-1301

2.54e-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: 2.54e-54

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   1172 FEPVVPLPDkIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHK-TSGKIRLLMRREQVLKICANHYISP 1250
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKdNGGKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   1251 DMKLTPNAGSDRSFVWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1301
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

cyclophilin

cd00317

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

3078-3219

5.75e-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: 5.75e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3078 GRITMELFSNIVPRTAENFRALCTGEkgfGFKNSIFHRVIPDFVCQGGDITkhDGTGGQSIYGDKFEDENFDVK-HTGPG 3156
Cdd:cd00317     7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyHHRRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150418007 3157 LLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFG-SPKGSVCRRITIT 3219
Cdd:cd00317    82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTIS 145

RanBD_family

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

2925-3041

4.96e-53

Pssm-ID: 269907 [Multi-domain] Cd Length: 118 Bit Score: 182.41 E-value: 4.96e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd00835     1 TGEENEEVLFEKRAKLFRFDKETKEWKERGVGDLKILKNKDTGKYRIVMRRDQVLKLCCNHYILPDMKLTKMGNNDRAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 3005 WTASDYAD-GEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd00835    81 WTAMDDSEdGEGKPETFAVRFKTAEDAEEFKKAFEEAQ 118

RanBD3_RanBP2-like

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

2027-2143

6.12e-53

Pssm-ID: 270204 Cd Length: 117 Bit Score: 182.09 E-value: 6.12e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd14685    81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

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

2027-2143

4.09e-52

Pssm-ID: 269999 Cd Length: 117 Bit Score: 179.77 E-value: 4.09e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD

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

2013-2142

7.64e-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: 179.51 E-value: 7.64e-52

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   2013 FEPVVQMPEkVELVTGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNG-KLRMLMRREQVLKVCANHWITT 2091
Cdd:smart00160    1 FKPVVPLPD-VEVKTGEEDEEVIFSARAKLYRFANDKKEWKERGVGDLKILKSKDNGgKVRIVMRRDGVLKVCANHPIFK 79

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 150418007   2092 TMNLKPLSGSDRAWMWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEEC 2142
Cdd:smart00160   80 SMTLKPLAGSNRALKWTPEDFADDIPKLVLYAVRFKTKEEADSFKNIFEEA 130

RanBD1_RanBP2-like

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

2027-2143

4.88e-51

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 176.76 E-value: 4.88e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

RanBD3_RanBP2-like

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

2925-3041

1.41e-50

Pssm-ID: 270204 Cd Length: 117 Bit Score: 175.15 E-value: 1.41e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd14685    81 WTAMDFAEGEGKIEQLAVRFKLQETADTFKQIFDEAK 117

RanBD4_RanBP2-like

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

2324-2440

1.98e-50

Pssm-ID: 269999 Cd Length: 117 Bit Score: 174.76 E-value: 1.98e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

RanBD2_RanBP2-like

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

2925-3041

1.42e-49

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 172.54 E-value: 1.42e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

RanBD2_RanBP2-like

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

1186-1302

1.92e-49

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 172.15 E-value: 1.92e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13177    81 WMANDFSDGDAKLEQLAAKFKTPELAEEFKLKFEECQ 117

Pro_isomerase

pfam00160

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

3077-3222

9.73e-49

Pssm-ID: 459694 [Multi-domain] Cd Length: 149 Bit Score: 171.28 E-value: 9.73e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  3077 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITkhdGTGGQSIYGDKFEDENFDVKHT-GP 3155
Cdd:pfam00160    6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPLLLKhKR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  3156 GLLSMANQGQ--NTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESfGSPKGSV-CRRITITECG 3222
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 ...

1186-1301

9.73e-49

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: 9.73e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFdvESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13171     1 TGEENEEVLFCARAKLFRY--VDKEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEA 1301
Cdd:cd13171    79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKA 114

RanBD3_RanBP2-like

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

1186-1302

5.59e-46

Pssm-ID: 270204 Cd Length: 117 Bit Score: 162.06 E-value: 5.59e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd14685     1 SGEENEQVVFSHRAKLYRYDKDAAQWKERGIGDLKILQNYDNKQVRLVMRRDQVLKLCANHRITADMKLQPMKGSERAWV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
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 ...

2926-3041

5.72e-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: 5.72e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2926 GEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVW 3005
Cdd:cd13174     2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3006 TASDYA-DGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13174    82 GGMNYAeDAEPEVETLAVRFKNEEIASQFKNVVDQCQ 118

YRB1

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

1951-2143

2.61e-45

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 164.04 E-value: 2.61e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1951 AKSTSGEGFQfgkKDPNFKGFSgAGEKLFSSQYGKMANKANTSGDFEK---DDDAYKTEDSDDIHFEPVVQMpEKVELVT 2027
Cdd:COG5171    10 AKIEKEENEQ---KERSLDVVS-KGDAFGDGKAGGEEKKVQQSPFLENavpEGDEGKGPESPNIHFEPVVEL-QRVHLKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2028 GEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWMW 2107
Cdd:COG5171    85 NEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVW 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 150418007 2108 L-ASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
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 ...

1186-1302

3.24e-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: 3.24e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKT-SGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSF 1264
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNKEdNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1265 VWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13172    81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD2_RanBP2-like

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

2324-2440

4.69e-45

Pssm-ID: 269998 [Multi-domain] Cd Length: 117 Bit Score: 159.44 E-value: 4.69e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd13177     1 TGEEDEKALYSQRVKLFRFDASVSQWKERGVGNLKILKNAVNGKLRMLMRREQVLKVCANHWITTTMNLKPLAGSDRAWM 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
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 ...

2027-2143

8.15e-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: 8.15e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKN-EVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAW 2105
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2106 MWLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
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 ...

2925-3041

1.06e-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: 1.06e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWH-TMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNAL 3003
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 3004 VWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
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 ...

2324-2440

4.20e-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: 4.20e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN-YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVW 2402
Cdd:cd13172     1 TGEENEEVLFEHRAKLLRFDKATKEWKERGLGNIKLLRNkEDNNKVRLLMRREQVLKVCCNQRLTKDMEFKYLTNNPKAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2403 LWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13172    81 TWCAQDYSEGELKPETFAIRFKTQEICKDFLDAVKKAQ 118

RanBD4_RanBP2-like

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

1186-1302

9.00e-44

Pssm-ID: 269999 Cd Length: 117 Bit Score: 155.88 E-value: 9.00e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13178     1 SGEEDEEILFKERAKLYRWDRDVGQWKERGVGDIKILFHPSKHYYRILMRRDQVLKVCANHVITQDMDLQPLSASNNTLV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13178    81 WTATDYADGEGKVEQLAVRFKTKEIADSFKKVFEECQ 117

YRB1

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

2849-3049

9.56e-44

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 159.41 E-value: 9.56e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2849 SFADLASSNSGDfAFGSKDKNFQWANTGAAVFGTQsvgtqsagKVGEDEDGSDEEvvhNEDIHFEPIVSLPEVEVKSGEE 2928
Cdd:COG5171    20 KERSLDVVSKGD-AFGDGKAGGEEKKVQQSPFLEN--------AVPEGDEGKGPE---SPNIHFEPVVELQRVHLKTNEE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2929 DEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVWT-A 3007
Cdd:COG5171    88 DETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsT 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 150418007 3008 SDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQNLMKLQK 3049
Cdd:COG5171   168 ADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQEHNEKALK 209

RanBD1_RanBP2-like

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

2925-3041

1.27e-43

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 155.57 E-value: 1.27e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd14684    81 WNALDYADELPKPEQLAIRFKTVEEAALFKCKFEEAQ 117

YRB1

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

1171-1304

1.92e-43

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 158.64 E-value: 1.92e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1171 HFEPVVPLpDKIEVKTGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISP 1250
Cdd:COG5171    70 HFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKHKKTNKARITMRRDKTLKLCANHFINP 148

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150418007 1251 DMKLTPNAGSDRSFVWH-ALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQSI 1304
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 ...

1186-1302

5.76e-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: 5.76e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13174     1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1266 WHALDYA-DELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
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 ...

2324-2440

1.01e-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: 1.01e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQnmKGTERVWL 2403
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVDK--EWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFR--KKDEKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
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 ...

2027-2141

2.16e-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: 2.16e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEvsQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYVDK--EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAYI 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2141
Cdd:cd13171    79 WAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTK 113

cyclophilin_RING

cd01923

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

3077-3209

1.20e-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: 1.20e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3155
Cdd:cd01923     8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150418007 3156 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPK 3209
Cdd:cd01923    84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPG 137

cyclophilin_SpCYP2_like

cd01922

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

3077-3202

1.36e-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: 1.36e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3155
Cdd:cd01922     6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 150418007 3156 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKI 3202
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 ...

1186-1303

1.57e-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: 1.57e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDveSKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNagSDRSFV 1265
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFV--DKEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKK--DEKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1266 WHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQS 1303
Cdd:cd13173    77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKN 114

RanBD1_RanBP2-like

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

2324-2440

9.86e-41

Pssm-ID: 270203 [Multi-domain] Cd Length: 117 Bit Score: 147.10 E-value: 9.86e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWL 2403
Cdd:cd14684     1 TGEEDEEEMFCNRAKLFRFDVETKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISADMKLKPNAGSDKSFV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2404 WTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
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 ...

2027-2143

1.61e-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: 1.61e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13174     1 TGEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFT 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2107 WLASDFS-DGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
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 ...

2027-2141

1.84e-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: 146.47 E-value: 1.84e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAevSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPlsGSDRAWM 2106
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRK--KDEKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150418007 2107 WLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2141
Cdd:cd13173    77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDD 111

PpiB

COG0652

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

3061-3204

2.85e-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: 2.85e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3061 ETNPVVFFDVcadgePLGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQsiyG 3140
Cdd:COG0652     4 APNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---G 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 3141 DKFEDENF-DVKHTgPGLLSMAN-QGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIES 3204
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 ...

2324-2440

4.36e-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: 4.36e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRY-DKdvgQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVW 2402
Cdd:cd13171     1 TGEENEEVLFCARAKLFRYvDK---EWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 2403 LWTACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13171    78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAK 115

Cyclophilin_PPIL3_like

cd01928

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

3077-3211

2.69e-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: 2.69e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCTGekGFgFKNSIFHRVIPDFVCQGGDITkHDGTGGQSIYGDKFEDENFD-VKHTGP 3155
Cdd:cd01928     9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREtLKHDSR 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 3156 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKGS 3211
Cdd:cd01928    85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKY 140

YRB1

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

2283-2445

4.82e-39

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

Pssm-ID: 227499 Cd Length: 211 Bit Score: 145.93 E-value: 4.82e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2283 KLNQSGTSVGTDEESDVTQEEERDGQYFEPVVPLpDLVEVSSGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQN 2362
Cdd:COG5171    44 KVQQSPFLENAVPEGDEGKGPESPNIHFEPVVEL-QRVHLKTNEEDETVLFKARAKLFRFDEEAKEWKERGTGDMIILKH 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2363 YDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLWT-ACDFADGERKVEHLAVRFKLQDVADSFKKIFDEAKT 2441
Cdd:COG5171   123 KKTNKARITMRRDKTLKLCANHFINPEFKLQPNVGSDRSWVWMsTADTVEGEAKAQTFAIRFYSEENAKRFKEEFEKGQE 202


                  ....
gi 150418007 2442 AQEK 2445
Cdd:COG5171   203 HNEK 206

RanBD1_RanBP2_insect-like

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

2925-3042

4.88e-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: 4.88e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWdrdVS-QWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNAL 3003
Cdd:cd13171     1 TGEENEEVLFCARAKLFRY---VDkEWKERGIGNLKILKNPATGKVRLLMRREQVHKVCANHFITKDMELTPMKKEDKAY 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 3004 VWTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQ 3042
Cdd:cd13171    78 IWAANDFADEVVVLEKLCVRFKTVELAKEFRDVFTKAKK 116

cyclophilin_WD40

cd01927

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

3077-3210

6.49e-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: 6.49e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFralCTGEKGFGFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3155
Cdd:cd01927     6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 150418007 3156 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFGSPKG 3210
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 ...

2325-2439

8.68e-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: 8.68e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2325 GEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWLW 2404
Cdd:cd13174     2 GEEDETKLFGERAKLYRFDADTKEWKERGVGEMKILYHPELNTYRLLMRREQVHKVVLNMLITSDLQLRPMNTSDKSFTW 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150418007 2405 TACDFA-DGERKVEHLAVRFKLQDVADSFKKIFDEA 2439
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 ...

2925-3043

4.42e-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: 4.42e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRdvSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNvsNNALV 3004
Cdd:cd13173     1 TGEEDEEVLYSHRAKLFRFVD--KEWKERGLGDVKILRHKETGKLRLLMRRDQVLKICLNHALTEELEFRKKD--EKSWM 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 3005 WTASDYADGEAKVEQLAVRFKTKEVADCFKKTFEECQQN 3043
Cdd:cd13173    77 WAAHDFSEGESELERFAIRFKNAEIAQGFMKAIDDAKNE 115

cyclophilin_CeCYP16-like

cd01925

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

3077-3192

6.22e-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: 6.22e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhDGTGGQSIYGDKFEDE-NFDVKHTGP 3155
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 3156 GLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFV 3192
Cdd:cd01925    90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126

IR1-M

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

2709-2769

1.13e-28

Pssm-ID: 463488 Cd Length: 60 Bit Score: 110.64 E-value: 1.13e-28

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 150418007  2709 ECIIVWEKKPTVEEKAKADTLKLPPTFFCGVCSDTDeDNGNGEDFQSELQKVQEAQKSQTE 2769
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFCGYSSDTD-DGDDLEDFETEVKKLNGKLYPDDE 60

cyclophilin_RRM

cd01921

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

3077-3219

1.18e-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: 1.18e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCTgEKGFGFknSIFHRVIPDFVCQGGDITkHDGTGGQSIYGDK-------FEDE-NF 3148
Cdd:cd01921     6 LGDLVIDLFTDECPLACLNFLKLCK-LKYYNF--CLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfFEPEiLP 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 150418007 3149 DVKHTGPGLLSMANQGQNTNNSQFVITLKKA-EHLDFKHVVFGFVKDGMDTVKKI-ESFGSPKGSVCRRITIT 3219
Cdd:cd01921    82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIK 154

PTZ00221

cyclophilin; Provisional

3066-3222

2.19e-22

cyclophilin; Provisional

Pssm-ID: 140248 Cd Length: 249 Bit Score: 99.17 E-value: 2.19e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3066 VFFDVCADGEPLGRITMELFSNIVPRTAENFRALCTGEKGF----GFKNSIFHRVIPDFVCQGGDITKHD-GTGGQSIYG 3140
Cdd:PTZ00221   55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdtntGVKLDYLYTPVHHVDRNNNIIVLGElDSFNVSSTG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3141 DKFEDENFDVKHTGPGLLSMANQGQNTNNSQFVITLKKAEHLDFKHVVFGFVKDGMDTVKKIESFgsPKGSVCR---RIT 3217
Cdd:PTZ00221  135 TPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL--PLDDVGRpllPVT 212


                  ....*
gi 150418007 3218 ITECG 3222
Cdd:PTZ00221  213 VSFCG 217

RanBD_NUP50

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

1186-1302

4.29e-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: 93.82 E-value: 4.29e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDvESKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSFV 1265
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 1266 WHALDyadelPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13170    80 CVPNP-----GKPVTYLLRVKTAEDADELAKALEEEK 111

RanBD_NUP50

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

2027-2143

3.23e-19

Pssm-ID: 269991 Cd Length: 111 Bit Score: 85.35 E-value: 3.23e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDaEVSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDrawm 2106
Cdd:cd13170     1 AGEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNN---- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 150418007 2107 wLASDFSDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13170    76 -VFVGCVPNPGKPVTYLLRVKTAEDADELAKALEEEK 111

cyclophilin_EcCYP_like

cd01920

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

3077-3204

1.53e-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: 1.53e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3077 LGRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHdgtGGQSIYGDKFEDENFDVKHTGPG 3156
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEAGNGLSNTRG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 150418007 3157 LLSMA-NQGQNTNNSQFVITLKKAEHLDFK-----HVVFGFVKDGMDTVKKIES 3204
Cdd:cd01920    80 TIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAG 133

RanBD_NUP50_plant

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

2324-2440

8.99e-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: 8.99e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKdvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMKGTERVWl 2403
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTF- 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 2404 wtAC--DFADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13169    78 --ACvnSAADAKDKLSTFALKFKDPQVVEEFRAAVEAHK 114

RanBD_NUP2

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

2027-2143

1.77e-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: 1.77e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQ--WKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPL-SGSDR 2103
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMgNGSLV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 150418007 2104 AWMWLasdfsDGDAKLEQLAAKFKTPELAEEFKQKFEECQ 2143
Cdd:cd13181    81 RVPTI-----NSDGKIETYVIKVKTAADGEELLKALNDAK 115

LapB

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

33-222

4.45e-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: 4.45e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDg 112
Cdd:COG2956    83 AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYD- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  113 RAKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEAE 192
Cdd:COG2956   162 EAIEALEKALKLDPDCARALLLLAELYLEQGD--YEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKAL 239

                         170       180       190
                  ....*....|....*....|....*....|
gi 150418007  193 RNIALRSSLEWNSCVVQTLKEYLESLQCLE 222
Cdd:COG2956   240 ELDPSDDLLLALADLLERKEGLEAALALLE 269

RanBD_RanBP3

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

2324-2435

4.72e-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: 4.72e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYDKDVGQWKERGIGDIKI--LQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQnmKGTERV 2401
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVE--KVSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|....
gi 150418007 2402 WLWTAcdfADGERKVEHLAVRFKLQDVADSFKKI 2435
Cdd:cd13180    79 LRITA---MDDEGQVKVFLLQASPEDAKQLYNAI 109

RanBD_NUP50

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

2325-2440

6.45e-16

Pssm-ID: 269991 Cd Length: 111 Bit Score: 76.10 E-value: 6.45e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2325 GEENEQVVFSHRAKLYRYDKDvGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTlqnMKGTERVWLW 2404
Cdd:cd13170     2 GEEEEDTVFEVRAKLFKKKDD-GEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMP---YSVAGKNNVF 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150418007 2405 TACDFADGerKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13170    78 VGCVPNPG--KPVTYLLRVKTAEDADELAKALEEEK 111

RanBD_RanBP3

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

2027-2099

2.05e-15

Pssm-ID: 270001 Cd Length: 113 Bit Score: 74.58 E-value: 2.05e-15

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAEVSQWKERGLGNLKILKNEVNGKL--RMLMRREQVLKVCANHWITTTMNLKPLS 2099
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLNDSKSDGSGqsRIVMRTQGSLRVILNTKIWPGMTVEKVS 75

IR1-M

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

2631-2693

2.77e-15

Pssm-ID: 463488 Cd Length: 60 Bit Score: 72.50 E-value: 2.77e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 150418007  2631 DVLIVYELTPTAEQKALATKLKLPPTFFCyknrpDYVSEEEEDDEDF--ETAVKKLNGKLYLDGS 2693
Cdd:pfam12185    1 ECVIVWEKKPTPEEKALAKTLQLPPTFFC-----GYSSDTDDGDDLEdfETEVKKLNGKLYPDDE 60

RanBD_NUP2

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

1186-1302

7.04e-15

Pssm-ID: 270002 Cd Length: 115 Bit Score: 73.24 E-value: 7.04e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKE--WKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPnAGSDRS 1263
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDPSNTEspYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEK-MGNGSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 1264 FVWHALDYADELpkpEQLAIRFKTPEEAALFKCKFEEAQ 1302
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 ...

2027-2141

7.45e-15

Pssm-ID: 269990 Cd Length: 117 Bit Score: 73.25 E-value: 7.45e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2027 TGEEDEKVLYSQRVKLFRFDAevSQWKERGLGNLKILKNEVNGKLRMLMRREQVLKVCANHWITTTMNLKPLSGSDRAWM 2106
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150418007 2107 WLASdFSDGDAKLEQLAAKFKTPELAEEFKQKFEE 2141
Cdd:cd13169    79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112

LapB

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

29-288

6.39e-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: 6.39e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   29 GFYF-AKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELL 104
Cdd:COG2956    10 GWYFkGLNYLLNGQPDKAIDL---LEEALELDPEtveAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  105 CKNDVTDgRAKYWLERAAKLFPGSPAIYklkEQLLDC---EGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRL 181
Cdd:COG2956    87 LKAGLLD-RAEELLEKLLELDPDDAEAL---RLLAEIyeqEGD--WEKAIEVLERLLKLGPENAHAYCELAELYLEQGDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  182 KDAVAHCHEA-------ERNIALRSSLEWNscvvqtLKEYLESLQCLEsdksDWRATNTDLLLAYANLMLLTLSTRDVQE 254
Cdd:COG2956   161 DEAIEALEKAlkldpdcARALLLLAELYLE------QGDYEEAIAALE----RALEQDPDYLPALPRLAELYEKLGDPEE 230

                         250       260       270
                  ....*....|....*....|....*....|....
gi 150418007  255 SRELLQsfdSALQSVKSLGGNDELSATFLEMKGH 288
Cdd:COG2956   231 ALELLR---KALELDPSDDLLLALADLLERKEGL 261

RanBD_RanBP3

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

1186-1263

6.63e-14

Pssm-ID: 270001 Cd Length: 113 Bit Score: 70.34 E-value: 6.63e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDVESKEWKERGIGNVKI--LRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPnaGSDRS 1263
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEK--VSEKS 78

RanBD_NUP50

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

2926-3041

8.82e-14

Pssm-ID: 269991 Cd Length: 111 Bit Score: 69.94 E-value: 8.82e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2926 GEEDEEILFKERAKLYRWDrDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALVW 3005
Cdd:cd13170     2 GEEEEDTVFEVRAKLFKKK-DDGEWKDKGVGTLRLKKHKTTGKARILVRADTLGKILLNFLLYKGMPYSVAGKNNVFVGC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 150418007 3006 TASDyadgeAKVEQLAVRFKTKEVADCFKKTFEECQ 3041
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 ...

1186-1301

1.91e-13

Pssm-ID: 269990 Cd Length: 117 Bit Score: 69.40 E-value: 1.91e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1186 TGEEDEEEFFCNRAKLFRFDveSKEWKERGIGNVKILRHKTSGKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRSF- 1264
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFI--DGGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFa 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1265 -VWHAldyADELPKPEQLAIRFKTPEEAALFKCKFEEA 1301
Cdd:cd13169    79 cVNSA---ADAKDKLSTFALKFKDPQVVEEFRAAVEAH 113

RanBD_NUP2

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

2925-3041

7.67e-13

Pssm-ID: 270002 Cd Length: 115 Bit Score: 67.46 E-value: 7.67e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWD--RDVSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNvsNNA 3002
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKMG--NGS 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 3003 LVWTASDYADGeaKVEQLAVRFKTKEVADCFKKTFEECQ 3041
Cdd:cd13181    79 LVRVPTINSDG--KIETYVIKVKTAADGEELLKALNDAK 115

RanBD_RanBP3

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

2925-3035

1.25e-12

Pssm-ID: 270001 Cd Length: 113 Bit Score: 66.87 E-value: 1.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRDVSQWKERGVGDIKI--LWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPlnVSNNA 3002
Cdd:cd13180     1 TGEEGETNVFQVNCKLYAFDKSKQSWKERGRGTLRLndSKSDGSGQSRIVMRTQGSLRVILNTKIWPGMTVEK--VSEKS 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 150418007 3003 LVWTASDyADGEAKVeqLAVRFKTKEVADCFKK 3035
Cdd:cd13180    79 LRITAMD-DEGQVKV--FLLQASPEDAKQLYNA 108

RanBD_NUP2

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

2324-2440

9.04e-12

Pssm-ID: 270002 Cd Length: 115 Bit Score: 64.38 E-value: 9.04e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2324 SGEENEQVVFSHRAKLYRYD--KDVGQWKERGIGDIKILQNYDNKQVRIVMRRDQVLKLCANHRITPDMTLQNMkGTERV 2401
Cdd:cd13181     1 TGEENEEVLYTKRAKLMLFDpsNTESPYTSKGVGELKLLKNKDTGKSRILVRAEGSLRVLLNTLVLKDVKYEKM-GNGSL 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 150418007 2402 WLWTAcdfADGERKVEHLAVRFKLQDVADSFKKIFDEAK 2440
Cdd:cd13181    80 VRVPT---INSDGKIETYVIKVKTAADGEELLKALNDAK 115

zf-RanBP

Zn-finger in Ran binding protein and others;

1781-1809

6.52e-11

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 59.29 E-value: 6.52e-11

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1781 RKGQWDCSVCCVQNESSSLKCVACDASKP 1809
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

BepA

COG4783

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

30-139

6.56e-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: 6.56e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDV 109
Cdd:COG4783     8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGD 87

                          90       100       110
                  ....*....|....*....|....*....|
gi 150418007  110 TDGRAKYWlERAAKLFPGSPAIYKLKEQLL 139
Cdd:COG4783    88 YDEALALL-EKALKLDPEHPEAYLRLARAY 116

TPR

COG0457

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

30-260

1.13e-10

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

Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 64.64 E-value: 1.13e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   30 FYFAKLYYEAKEYDLAKKYictY---INVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK 106
Cdd:COG0457    12 NNLGLAYRRLGRYEEAIED---YekaLELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  107 ndvtDGR---AKYWLERAAKLFPGSPAIYKLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKD 183
Cdd:COG0457    89 ----LGRyeeALEDYDKALELDPDDAEALYNLGLALLELGR--YDEAIEAYERALELDPDDADALYNLGIALEKLGRYEE 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 150418007  184 AVAHCHEAERNIALRSSLEWNSCVVQTLKEYLESLQCLESDKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQ 260
Cdd:COG0457   163 ALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALA 239

zf-RanBP

Zn-finger in Ran binding protein and others;

1479-1508

1.33e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 58.13 E-value: 1.33e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1479 KEGQWDCSACLVQNEGSSTKCAACQNPRKQ 1508
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1606-1635

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1606 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1635
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1665-1694

1.84e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 57.75 E-value: 1.84e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1665 KEGQWDCSVCLVRNEASATKCIACQNPGKQ 1694
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

PRK10903

peptidylprolyl isomerase A;

3078-3202

3.33e-10

peptidylprolyl isomerase A;

Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 62.17 E-value: 3.33e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3078 GRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHdgtGGQSIYGDKFEDENFDVKHTGPGL 3157
Cdd:PRK10903   38 GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFTEQ---MQQKKPNPPIKNEADNGLRNTRGT 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 150418007 3158 LSMANQG-QNTNNSQFVITLKKAEHL-----DFKHVVFGFVKDGMDTVKKI 3202
Cdd:PRK10903  112 IAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKI 162

zf-RanBP

Zn-finger in Ran binding protein and others;

1543-1572

5.28e-10

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 56.59 E-value: 5.28e-10

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1543 KEGQWDCSSCLVRNEANATRCVACQNPDKP 1572
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

zf-RanBP

Zn-finger in Ran binding protein and others;

1724-1753

1.25e-09

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 55.44 E-value: 1.25e-09

                           10        20        30
                   ....*....|....*....|....*....|
gi 150418007  1724 KEGQWDCSVCLVRNEASATKCIACQCPSKQ 1753
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30

PRK10791

peptidylprolyl isomerase B;

3078-3204

1.83e-08

peptidylprolyl isomerase B;

Pssm-ID: 182734 Cd Length: 164 Bit Score: 56.39 E-value: 1.83e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3078 GRITMELFSNIVPRTAENFRALCTgeKGFgFKNSIFHRVIPDFVCQGGDITKhdGTGGQSIYGDKFEDENFDVKHTgPGL 3157
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGFEP--GMKQKATKEPIKNEANNGLKNT-RGT 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 150418007 3158 LSMA-NQGQNTNNSQFVITLKKAEHLDFK--------HVVFGFVKDGMDTVKKIES 3204
Cdd:PRK10791   83 LAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKG 138

PH-like

cd00900

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

1195-1298

2.69e-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: 2.69e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1195 FCNRAKLFRFdveskEWKERGIGNVKILrhktsgKIRLLMRREQVLKICANHYISPDMKLTPNAGSDRS--FVWHALDya 1272
Cdd:cd00900     1 LKFRAVRVYR-----EPTKRVEGTLYIT------SDRLILRDKNDGGLELSIPISDIVNVNVSPQGPSSryLVLVLKD-- 67

                          90       100
                  ....*....|....*....|....*.
gi 150418007 1273 delpKPEQLAIRFKTPEEAALFKCKF 1298
Cdd:cd00900    68 ----RGEFVGFSFPKEEDAIEISDAL 89

zf-RanBP

Zn-finger in Ran binding protein and others;

1415-1443

3.05e-08

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 51.58 E-value: 3.05e-08

                           10        20
                   ....*....|....*....|....*....
gi 150418007  1415 KEGHWDCSICLVRNEPTVSRCIACQNTKS 1443
Cdd:pfam00641    1 REGDWDCSKCLVQNFATSTKCVACQAPKP 29

TPR

COG0457

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

53-298

5.44e-08

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

Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 56.55 E-value: 5.44e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   53 INVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAIY 132
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYE-EALADYEQALELDPDDAEAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  133 KLKEQLLDCEGEdgWNKLFDLIQSELYVRPDDVHVNIRLVEVYRSTKRLKDAVAHCHEA-ERNIALRSSLEWNSCVVQTL 211
Cdd:COG0457    80 NNLGLALQALGR--YEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAlELDPDDADALYNLGIALEKL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  212 KEYLESLQCLEsdKSDWRATNTDLLLAYANLMLLTLSTRDVQESRELLQSFDSALQSVKSLGGNDELSATFLEMKGHFYM 291
Cdd:COG0457   158 GRYEEALELLE--KLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRL 235


                  ....*..
gi 150418007  292 HAGSLLL 298
Cdd:COG0457   236 AALALYQ 242

TadD

COG5010

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

35-126

5.82e-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: 5.82e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   35 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 114
Cdd:COG5010    63 LYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDD-EA 141

                          90
                  ....*....|..
gi 150418007  115 KYWLERAAKLFP 126
Cdd:COG5010   142 KAALQRALGTSP 153

NrfG

COG4235

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

59-132

9.32e-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: 9.32e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150418007   59 DPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAIY 132
Cdd:COG4235    16 DAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTE-EAEELLERALALDPDNPEAL 88

PilF

COG3063

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

35-126

7.22e-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: 7.22e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   35 LYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVEcYRRSVELNPTQKDLVLKIAELLCKNDVTDgRA 114
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYD-EA 78

                          90
                  ....*....|..
gi 150418007  115 KYWLERAAKLFP 126
Cdd:COG3063    79 LAYLERALELDP 90

cyclophilin_TLP40_like

cd01924

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

3078-3203

7.47e-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: 7.47e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3078 GRITMELFSNIVPRTAENFRALCtgEKGFgFKNSIFHRVIPDFVCQGGDITKHD------GTG--------------GQS 3137
Cdd:cd01924     7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 3138 IYGDKFE-----DENFDVKHTGPGLLSMANQ--GQNTNNSQFVITLKKAEH-------LDFKHVVFGFVKDGMDTVKKIE 3203
Cdd:cd01924    84 VYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLDILRELK 163

zf-RanBP

Zn-finger in Ran binding protein and others;

1351-1381

7.79e-07

Zn-finger in Ran binding protein and others;

Pssm-ID: 395516 [Multi-domain] Cd Length: 30 Bit Score: 47.73 E-value: 7.79e-07

                           10        20        30
                   ....*....|....*....|....*....|.
gi 150418007  1351 KEGsWWHCNSCSLKNASTAKKCVSCQNLNPS 1381
Cdd:pfam00641    1 REG-DWDCSKCLVQNFATSTKCVACQAPKPD 30

CpoB

COG1729

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

34-138

1.10e-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: 1.10e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   34 KLYYEAKEYDLAKKYictYINVQERDPK------AHRFLGLLYELEENTDKAVECYRRSVELNPTQK---DLVLKIAELL 104
Cdd:COG1729     1 KALLKAGDYDEAIAA---FKAFLKRYPNsplapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPkapDALLKLGLSY 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 150418007  105 CKNDVTDgRAKYWLERAAKLFPGSPAIYKLKEQL 138
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 ...

2925-3039

2.01e-06

Pssm-ID: 269990 Cd Length: 117 Bit Score: 48.98 E-value: 2.01e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 2925 SGEEDEEILFKERAKLYRWDRdvSQWKERGVGDIKILWHTMKNYYRILMRRDQVFKVCANHVITKTMELKPLNVSNNALV 3004
Cdd:cd13169     1 TGEENEKAVFSGDGALFEFID--GGWKERGKGELRVNLSTTTGQARLVMRARGNYRLILNANLYPDMKLTKMGGKGVTFA 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 150418007 3005 WTASdYADGEAKVEQLAVRFKTKEVADCFKKTFEE 3039
Cdd:cd13169    79 CVNS-AADAKDKLSTFALKFKDPQVVEEFRAAVEA 112

BepA

COG4783

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

31-126

3.71e-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: 3.71e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   31 YFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVT 110
Cdd:COG4783    43 LLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRP 122

                          90
                  ....*....|....*.
gi 150418007  111 DGRAKYWlERAAKLFP 126
Cdd:COG4783   123 DEAIAAL-EKALELDP 137

ZnF_RBZ

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

1667-1691

6.94e-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: 6.94e-06

                            10        20
                    ....*....|....*....|....*
gi 150418007   1667 GQWDCSVCLVRNEASATKCIACQNP 1691
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

ZnF_RBZ

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

1608-1632

6.94e-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: 6.94e-06

                            10        20
                    ....*....|....*....|....*
gi 150418007   1608 GQWDCSVCLVRNEASATKCIACQNP 1632
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

BepA

COG4783

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

30-93

9.97e-06

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

Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 47.88 E-value: 9.97e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 150418007   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQ 93
Cdd:COG4783    76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139

ZnF_RBZ

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

1726-1748

5.27e-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: 5.27e-05

                            10        20
                    ....*....|....*....|...
gi 150418007   1726 GQWDCSVCLVRNEASATKCIACQ 1748
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACG 23

ZnF_RBZ

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

1783-1807

7.58e-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: 7.58e-05

                            10        20
                    ....*....|....*....|....*
gi 150418007   1783 GQWDCSVCCVQNESSSLKCVACDAS 1807
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TadD

COG5010

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

33-91

1.18e-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: 1.18e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 150418007   33 AKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 91
Cdd:COG5010    95 ALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153

ZnF_RBZ

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

1481-1505

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 150418007   1481 GQWDCSACLVQNEGSSTKCAACQNP 1505
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR

smart00028

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

60-92

1.35e-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: 1.35e-04

                            10        20        30
                    ....*....|....*....|....*....|...
gi 150418007     60 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 92
Cdd:smart00028    1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33

Spy

COG3914

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

32-267

1.41e-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: 1.41e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   32 FAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK-NDVT 110
Cdd:COG3914    84 AALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRlGRLE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  111 DGRAKYwlERAAKLFPGSPAIYklkeqlldcegedgwnklfdliqselyvrpddvhvnIRLVEVYRSTKRLKDAVAHCHE 190
Cdd:COG3914   164 EAIAAL--RRALELDPDNAEAL------------------------------------NNLGNALQDLGRLEEAIAAYRR 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007  191 AER----NIALRSSLE---WNSCVVQTLKEYLESLQCLESDKSDWratntdlllayANLMLLTLSTRDVQESRELLQSFD 263
Cdd:COG3914   206 ALEldpdNADAHSNLLfalRQACDWEVYDRFEELLAALARGPSEL-----------SPFALLYLPDDDPAELLALARAWA 274


                  ....
gi 150418007  264 SALQ 267
Cdd:COG3914   275 QLVA 278

Spy

COG3914

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

30-132

1.42e-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: 1.42e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCK-ND 108
Cdd:COG3914   116 FNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDlGR 195

                          90       100
                  ....*....|....*....|....
gi 150418007  109 VTDGRAkyWLERAAKLFPGSPAIY 132
Cdd:COG3914   196 LEEAIA--AYRRALELDPDNADAH 217

ZnF_RBZ

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

1545-1569

1.50e-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: 1.50e-04

                            10        20
                    ....*....|....*....|....*
gi 150418007   1545 GQWDCSSCLVRNEANATRCVACQNP 1569
Cdd:smart00547    1 GDWECPACTFLNFASRSKCFACGAP 25

TPR_1

pfam00515

Tetratricopeptide repeat;

60-92

1.74e-04

Tetratricopeptide repeat;

Pssm-ID: 459840 [Multi-domain] Cd Length: 34 Bit Score: 40.87 E-value: 1.74e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 150418007    60 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 92
Cdd:pfam00515    1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33

PEP_TPR_lipo

TIGR02917

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

30-291

1.91e-04

Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 47.39 E-value: 1.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007    30 FYFAKLYYEAKEYDLAKKYictYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAE-LLC 105
Cdd:TIGR02917  503 ANLARIDIQEGNPDDAIQR---FEKVLTIDPKnlrAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQyYLG 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   106 KNDVtdGRAKYWLERAAKLFPGSPAIYKLK--EQLLDCEGEDGWNKLFDLIQselyVRPDDVHVNIRLVEVYRSTKRLKd 183
Cdd:TIGR02917  580 KGQL--KKALAILNEAADAAPDSPEAWLMLgrAQLAAGDLNKAVSSFKKLLA----LQPDSALALLLLADAYAVMKNYA- 652

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   184 avahchEAERniALRSSLEWnscvvqtlkeyleslqclesdKSDwratNTDLLLAYANLMLLTlstrdvqesrellQSFD 263
Cdd:TIGR02917  653 ------KAIT--SLKRALEL---------------------KPD----NTEAQIGLAQLLLAA-------------KRTE 686

                          250       260
                   ....*....|....*....|....*...
gi 150418007   264 SALQSVKSLGGNDELSATFLEMKGHFYM 291
Cdd:TIGR02917  687 SAKKIAKSLQKQHPKAALGFELEGDLYL 714

NrfG

COG4235

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

30-91

3.44e-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: 3.44e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 150418007   30 FYFAKLYYEAKEYDLAKKYICTYINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNP 91
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 ...

1188-1302

4.29e-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: 4.29e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007 1188 EEDEEEF-FCNRAKLFRFDVESKEWKERGIGNVKILRHKT--SGKIRLLMRREQVlkICANHYISPDMKLTPnagSDRSF 1264
Cdd:cd13175     2 DDDEELFmFEKRITLEMLIGNGNKWLDLGQGNLRIVYDDEiyGARIVLSDDDTDT--IIANTIIAVQTSLRV---EGKEA 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 150418007 1265 VWHALDYADELPKPEQLAIRFKTPEEAALFKCKFEEAQ 1302
Cdd:cd13175    77 IWSAIDYSQEPLLRRRFRAEFSSDDAAQEFSVVFNEGK 114

TPR_2

pfam07719

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

60-92

6.30e-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: 6.30e-04

                           10        20        30
                   ....*....|....*....|....*....|...
gi 150418007    60 PKAHRFLGLLYELEENTDKAVECYRRSVELNPT 92
Cdd:pfam07719    1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33

NlpI

COG4785

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

35-129

6.90e-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: 6.90e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   35 LYYEAKEYDLAkkyICTYINVQERDPK---AHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLK--IAELLckndv 109
Cdd:COG4785    82 AYDSLGDYDLA---IADFDQALELDPDlaeAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNrgIALYY----- 153

                          90       100
                  ....*....|....*....|...
gi 150418007  110 tDGR---AKYWLERAAKLFPGSP 129
Cdd:COG4785   154 -LGRyelAIADLEKALELDPNDP 175

TadD

COG5010

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

52-139

9.19e-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: 9.19e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 150418007   52 YINVQERDPKAHRFLGLLYELEENTDKAVECYRRSVELNPTQKDLVLKIAELLCKNDVTDgRAKYWLERAAKLFPGSPAI 131
Cdd:COG5010    46 GRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKD-EAKEYYEKALALSPDNPNA 124


                  ....*...
gi 150418007  132 YKLKEQLL 139
Cdd:COG5010   125 YSNLAALL 132

ZnF_RBZ