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Conserved domains on  [gi|46852172|ref|NP_056069|]
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kinesin-like protein KIF13B [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


:

Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365  160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365  240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 46852172  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365  320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 4.18e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


:

Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730    1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                         90
                 ....*....|....*....
gi 46852172  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730   81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 1704-1767 3.26e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.26e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46852172   1704 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1767
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
Kinesin_assoc super family cl24686
Kinesin-associated;
357-469 7.11e-25

Kinesin-associated;


The actual alignment was detected with superfamily member pfam16183:

Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.38  E-value: 7.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 46852172    455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 1.95e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


:

Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.95e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172    756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1424-1683 1.28e-11

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.35  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1492
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1493 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1569
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1570 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1641
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 46852172  1642 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1683
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
DUF3694 super family cl13857
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 7.82e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


The actual alignment was detected with superfamily member pfam12473:

Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.28  E-value: 7.82e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852172   1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
bMERB_dom super family cl48129
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 1.31e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


The actual alignment was detected with superfamily member pfam12130:

Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172   1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913  612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365  160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365  240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 46852172  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365  320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-360 2.39e-156

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 482.07  E-value: 2.39e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172       6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172      86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 46852172     326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 8.25e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 461.27  E-value: 8.25e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301

                          330       340
                   ....*....|....*....|....*
gi 46852172    329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 8.13e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 319.38  E-value: 8.13e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059   52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059  124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059  201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059  277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059  353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432


                 ...
gi 46852172  437 QSS 439
Cdd:COG5059  433 QFL 435
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-379 4.34e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.21  E-value: 4.34e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188  153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188  233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188  311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172   309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188  390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 4.18e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730    1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                         90
                 ....*....|....*....
gi 46852172  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730   81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 1704-1767 3.26e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.26e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46852172   1704 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1767
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 1704-1768 5.92e-26

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 102.28  E-value: 5.92e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172    1704 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1768
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 7.11e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.38  E-value: 7.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 46852172    455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 1.95e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.95e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172    756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 1704-1773 4.52e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 74.34  E-value: 4.52e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1704 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1773
Cdd:COG5244    7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1424-1683 1.28e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.35  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1492
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1493 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1569
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1570 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1641
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 46852172  1642 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1683
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 471-534 3.70e-11

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 60.28  E-value: 3.70e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46852172    471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 1439-1753 5.85e-08

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.77  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1439 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1518
Cdd:COG5180  174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1519 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1593
Cdd:COG5180  253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1594 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1657
Cdd:COG5180  332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1658 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1735
Cdd:COG5180  412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484

                        330
                 ....*....|....*...
gi 46852172 1736 DLPSGKNDGSIGGKQYFR 1753
Cdd:COG5180  485 LGVRPDAILGGNVAPASG 502
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 1476-1655 1.86e-07

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 55.56  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1476 RGKRPSPLAHQP-----VPRIMVQSASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI------- 1542
Cdd:pfam13254  165 KPKAQPSQPAQPawmkeLNKIRQSRASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeep 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1543 AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPP 1622
Cdd:pfam13254  238 SEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKAS 315

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 46852172   1623 GPQQLVSPGRErPDLEAPAPGSP---FRV---RRVRASE 1655
Cdd:pfam13254  316 IDKPLSSPDRD-PLSPKPKPQSPpkdFRAnlrSREVPKD 353
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 7.82e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.28  E-value: 7.82e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852172   1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1533-1654 8.68e-06

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 50.15  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1533 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1604
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46852172  1605 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1654
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 1.14e-05

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 1.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716   20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 1.31e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172   1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1424-1645 2.63e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 45.92  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1503
Cdd:NF033839  294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1504 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1582
Cdd:NF033839  356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172  1583 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1645
Cdd:NF033839  411 -PQPEKPKPevkPQPEKPKPEVKPQ-----PEKPKPEVKPQPEKPKPEVKPQPETPKPEVkPQPEKP 471
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 1505-1641 4.14e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 42.76  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1505 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1573
Cdd:cd21975   12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46852172 1574 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1641
Cdd:cd21975   88 SLESGDADMGSDSDVAPASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 1579-1663 7.91e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.22  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1579 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1655
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101


                  ....*...
gi 46852172  1656 LRSFSRML 1663
Cdd:NF041121  102 PLELARAL 109
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1539-1645 1.69e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 42.83  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1539 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1614
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273

                          90       100       110
                  ....*....|....*....|....*....|.
gi 46852172  1615 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1645
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 1532-1699 1.86e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.14  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1532 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1603
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1604 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1677
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447

                          170       180
                   ....*....|....*....|...
gi 46852172   1678 PA-PGAGGQALASDSEEADEVPE 1699
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
 368-444 2.00e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 41.89  E-value: 2.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46852172  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493   36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 2.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172   368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913  612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
 
Name Accession Description Interval E-value
KISc_KIF1A_KIF1B cd01365
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ...
 4-360 0e+00

Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.


Pssm-ID: 276816 [Multi-domain]  Cd Length: 361  Bit Score: 601.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNLSKGDARGQPKVFAYDHCFWSMDeSVKEKYAGQDIVFKC 82
Cdd:cd01365    1 ANVKVAVRVRPFNSREKERNSKCIVQMSGKETTLkNPKQADKNNKATREVPKSFSFDYSYWSHD-SEDPNYASQEQVYED 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01365   80 LGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVSYMEIYNEKVRDLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  163 DPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSG 240
Cdd:cd01365  160 NPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDAETN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  241 TSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01365  240 LTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSFIPYRDSVLTWLLKENL 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 46852172  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:cd01365  320 GGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
 6-360 2.39e-156

Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.


Pssm-ID: 214526 [Multi-domain]  Cd Length: 335  Bit Score: 482.07  E-value: 2.39e-156
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172       6 VKVAVRIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGE 85
Cdd:smart00129    2 IRVVVRVRPLNKREKSRKSPSVVPFPDKV----GKTLTVRSPKNRQGEKKFTFDKVF---DAT-----ASQEDVFEETAA 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172      86 NILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYMEIYNEKVRDLLDPk 165
Cdd:smart00129   70 PLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLEIYNEKIRDLLNP- 147

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     166 gSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSgeK 245
Cdd:smart00129  148 -SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSG--K 224

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     246 VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTWLLKDSLGGNSKTA 325
Cdd:smart00129  225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTRLLQDSLGGNSKTL 300

                           330       340       350
                    ....*....|....*....|....*....|....*
gi 46852172     326 MVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 360
Cdd:smart00129  301 MIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
11-353 8.25e-149

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 461.27  E-value: 8.25e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     11 RIRPMNRRETDLHTKCVVDVDANKvilnPVNTNLSKGDARGQPKVFAYDHCFWSmdesvkekYAGQDIVFKCLGENILQN 90
Cdd:pfam00225    1 RVRPLNEREKERGSSVIVSVESVD----SETVESSHLTNKNRTKTFTFDKVFDP--------EATQEDVYEETAKPLVES 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     91 AFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIYNEKVRDLLDPKGSRQ- 169
Cdd:pfam00225   69 VLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKr 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    170 TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGTSGeKVGKL 249
Cdd:pfam00225  148 KLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESV-KTGKL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    250 SLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVA 328
Cdd:pfam00225  227 NLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIA 301

                          330       340
                   ....*....|....*....|....*
gi 46852172    329 TVSPAADNYDETLSTLRYADRAKHI 353
Cdd:pfam00225  302 NISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
 5-351 3.48e-142

Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276812 [Multi-domain]  Cd Length: 326  Bit Score: 442.85  E-value: 3.48e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRRETDLhTKCVVDVDANK-VILNPvntnlsKGDARGQPKVFAYDHCFWSMdesvkekyAGQDIVFKCL 83
Cdd:cd00106    1 NVRVAVRVRPLNGREARS-AKSVISVDGGKsVVLDP------PKNRVAPPKTFAFDAVFDST--------STQEEVYEGT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLL 162
Cdd:cd00106   66 AKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLEIYNEKIYDLL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  163 DPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHtlYDVKSGTS 242
Cdd:cd00106  146 SPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd00106  223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTRLLQDSLGGNS 297

                        330       340
                 ....*....|....*....|....*....
gi 46852172  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd00106  298 KTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
 6-353 1.53e-119

Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276822 [Multi-domain]  Cd Length: 334  Bit Score: 380.65  E-value: 1.53e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    6 VKVAVRIRPMNRRETDLHTKCVVDVDankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmDESVKEkYAGQDIVFKCLGE 85
Cdd:cd01371    3 VKVVVRCRPLNGKEKAAGALQIVDVD---EKRGQVSVRNPKATANEPPKTFTFDAVF---DPNSKQ-LDVYDETARPLVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   86 NILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:cd01371   76 SVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEIYNEEIRDLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  163 DpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlYDVKSGTS 242
Cdd:cd01371  151 G-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS-EKGEDGEN 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01371  229 HIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRLLQDSLGGNS 303

                        330       340       350
                 ....*....|....*....|....*....|.
gi 46852172  323 KTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01371  304 KTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
 5-355 5.43e-112

Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276817 [Multi-domain]  Cd Length: 329  Bit Score: 359.22  E-value: 5.43e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVILNpvntnLSKGDARgqPKVFAYDHCFwSMDESvkekyagQDIVFKCLg 84
Cdd:cd01366    3 NIRVFCRVRPLLPSEENEDTSHITFPDEDGQTIE-----LTSIGAK--QKEFSFDKVF-DPEAS-------QEDVFEEV- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEIYNEKVRDLLDP 164
Cdd:cd01366   67 SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEIYNETIRDLLAP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  165 KGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvkSGT- 241
Cdd:cd01366  147 GNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI--------SGRn 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  242 --SGEK-VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRDSVLTWLLKDSL 318
Cdd:cd01366  219 lqTGEIsVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRNSKLTYLLQDSL 292

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 46852172  319 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVN 355
Cdd:cd01366  293 GGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
 6-353 7.32e-111

Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276821 [Multi-domain]  Cd Length: 345  Bit Score: 356.65  E-value: 7.32e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    6 VKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNP----------VNTNLSKGDARGQPKVFAYDHCFwsmDEsvkekYA 74
Cdd:cd01370    2 LTVAVRVRPFSEKEKNEGFRRIVKVmDNHMLVFDPkdeedgffhgGSNNRDRRKRRNKELKYVFDRVF---DE-----TS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   75 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEIY 154
Cdd:cd01370   74 TQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLEIY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  155 NEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTl 234
Cdd:cd01370  153 NETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  235 YDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTWLL 314
Cdd:cd01370  230 DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTRLL 306

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 46852172  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01370  307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
 3-353 2.36e-110

Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276820 [Multi-domain]  Cd Length: 325  Bit Score: 354.33  E-value: 2.36e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    3 DSKVKVAVRIRPMNRRETDLHTKCVVDVDankvilnPVNTNLSKGDARGqpKVFAYDHCFwSMDesvkekyAGQDIVFKC 82
Cdd:cd01369    1 ECNIKVVCRFRPLNELEVLQGSKSIVKFD-------PEDTVVIATSETG--KTFSFDRVF-DPN-------TTQEDVYNF 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEIYNEKVR 159
Cdd:cd01369   64 AAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSYFEIYMEKIR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  160 DLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTlyDVKS 239
Cdd:cd01369  143 DLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE--NVET 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  240 GTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWLLKDSLG 319
Cdd:cd01369  219 EKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKLTRILQDSLG 291

                        330       340       350
                 ....*....|....*....|....*....|....
gi 46852172  320 GNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01369  292 GNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
 4-353 6.67e-110

Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276823 [Multi-domain]  Cd Length: 341  Bit Score: 353.56  E-value: 6.67e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    4 SKVKVAVRIRPMNRRETDLHTKCVVDVDANK--VILnpvntnlskgdarGQPKVFAYDHCFWSMDEsvkekyagQDIVFK 81
Cdd:cd01372    1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEpqVTV-------------GTDKSFTFDYVFDPSTE--------QEEVYN 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 155
Cdd:cd01372   60 TCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKVSFLEIYN 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  156 EKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTL 234
Cdd:cd01372  139 EEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTK 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  235 YDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNKFVPYRDS 308
Cdd:cd01372  219 KNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGAHVPYRDS 295

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 46852172  309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01372  296 KLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
 5-353 1.05e-108

Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276825 [Multi-domain]  Cd Length: 321  Bit Score: 349.32  E-value: 1.05e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIL-NPVNTNlskgdargqpkvFAYDHCFwSMDESVKEkyagqdiVFKCL 83
Cdd:cd01374    1 KITVTVRVRPLNSREIGINEQVAWEIDNDTIYLvEPPSTS------------FTFDHVF-GGDSTNRE-------VYELI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   84 GENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKVRDLLD 163
Cdd:cd01374   61 AKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKINDLLS 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  164 PKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVKSGtSG 243
Cdd:cd01374  139 PTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEE-GT 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  244 EKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSLGGNSK 323
Cdd:cd01374  216 VRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSLGGNSR 291

                        330       340       350
                 ....*....|....*....|....*....|
gi 46852172  324 TAMVATVSPAADNYDETLSTLRYADRAKHI 353
Cdd:cd01374  292 TAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
 6-362 1.33e-100

Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276824 [Multi-domain]  Cd Length: 347  Bit Score: 327.54  E-value: 1.33e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    6 VKVAVRIRPMNRRETDL-HTKCVVDVDANKVILNPVntnlskgdargQPKVFAYDHcfwsmdesVKEKYAGQDIVFKCLG 84
Cdd:cd01373    3 VKVFVRIRPPAEREGDGeYGQCLKKLSSDTLVLHSK-----------PPKTFTFDH--------VADSNTNQESVFQSVG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSFKVEVSYMEI 153
Cdd:cd01373   64 KPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSFLCKCSFLEI 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  154 YNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 233
Cdd:cd01373  144 YNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  234 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVPYRDSVLTWL 313
Cdd:cd01373  221 -WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VCYRDSKLTFL 297

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 46852172  314 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01373  298 LRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
 3-362 5.04e-95

Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276815 [Multi-domain]  Cd Length: 353  Bit Score: 311.57  E-value: 5.04e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    3 DSKVKVAVRIRPMNRRETDLHTKCVVDV-DANKVILNPVNTNLSKGDArgqpKVFAYDHCFWSmdesvkekYAGQDIVFK 81
Cdd:cd01364    1 GKNIQVVVRCRPFNLRERKASSHSVVEVdPVRKEVSVRTGGLADKSST----KTYTFDMVFGP--------EAKQIDVYR 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   82 CLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFERTqkeENEEQSFKVEVSY 150
Cdd:cd01364   69 SVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGTEYSVKVSY 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  151 MEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 227
Cdd:cd01364  146 LEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  228 ITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagknKNKFVP 304
Cdd:cd01364  226 ITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE------RAPHVP 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172  305 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 362
Cdd:cd01364  296 YRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
50-439 8.13e-95

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 319.38  E-value: 8.13e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   50 RGQPKVFAYDHCFwsmDESvkekyAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSG 129
Cdd:COG5059   52 KSKEGTYAFDKVF---GPS-----ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKE 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  130 LFERTQKEeNEEQSFKVEVSYMEIYNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRT 209
Cdd:COG5059  124 LFSKLEDL-SMTKDFAVSISYLEIYNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  210 VAATNMNEESSRSHAVFKITLTHtlYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISA 289
Cdd:COG5059  201 TASTEINDESSRSHSIFQIELAS--KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINA 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  290 LADqsagKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPN 364
Cdd:COG5059  277 LGD----KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREI 352

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  365 ARIIRDL---REEVEKLREQLTKAEAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISL 436
Cdd:COG5059  353 EEIKFDLsedRSEIEILVFREQSQLSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTL 432


                 ...
gi 46852172  437 QSS 439
Cdd:COG5059  433 QFL 435
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
 5-351 4.90e-79

Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276819 [Multi-domain]  Cd Length: 345  Bit Score: 265.41  E-value: 4.90e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRRETDLHTK-CVVDVDANKVILNPVNTNLSKGDARG---QPKVFAYDHCFwSMDESVKEKYAGqdiVF 80
Cdd:cd01368    2 PVKVYLRVRPLSKDELESEDEgCIEVINSTTVVLHPPKGSAANKSERNggqKETKFSFSKVF-GPNTTQKEFFQG---TA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   81 KCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEIYNEKVRD 160
Cdd:cd01368   78 LPLVQDLLH----GKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEIYNEYIYD 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  161 LLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL----T 231
Cdd:cd01368  147 LLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapG 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  232 HTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVPYRDSVLT 311
Cdd:cd01368  227 DSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVPFRDSKLT 305

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 46852172  312 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01368  306 HLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
 3-379 4.34e-77

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 282.21  E-value: 4.34e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172     3 DSKVKVAVRIRPMNRRETDlhtkcvvDVDANKVILNPVNTNlskgdarGQpkVFAYDhcfwsmdeSVKEKYAGQDIVFKC 82
Cdd:PLN03188   97 DSGVKVIVRMKPLNKGEEG-------EMIVQKMSNDSLTIN-------GQ--TFTFD--------SIADPESTQEDIFQL 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQKEE----NEEQSFKVEV 148
Cdd:PLN03188  153 VGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhaDRQLKYQCRC 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   149 SYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 228
Cdd:PLN03188  233 SFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTC 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   229 TLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgKNKNKFVPYRDS 308
Cdd:PLN03188  311 VVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQ-TGKQRHIPYRDS 389

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172   309 VLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--ARIIRDLREEVEKLR 379
Cdd:PLN03188  390 RLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflREVIRQLRDELQRVK 466
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
 5-351 8.25e-75

Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276826 [Multi-domain]  Cd Length: 334  Bit Score: 252.89  E-value: 8.25e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRREtdlHTKCVVDVDaNKVILNPVNTNLSKGDARGQPKVFAYdhcfwSMDESVKEkyAGQDIVFKCLG 84
Cdd:cd01375    1 KVQAFVRVRPTDDFA---HEMIKYGED-GKSISIHLKKDLRRGVVNNQQEDWSF-----KFDGVLHN--ASQELVYETVA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   85 ENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSYMEIYNEKVRDL 161
Cdd:cd01375   70 KDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSYLEIYNEQLYDL 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  162 LDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL---THTL 234
Cdd:cd01375  148 LSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLeahSRTL 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  235 YDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFVPYRDSVLTWLL 314
Cdd:cd01375  228 SSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHVPFRQSKLTHVL 297

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 46852172  315 KDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01375  298 RDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
 5-351 2.34e-74

Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276818 [Multi-domain]  Cd Length: 328  Bit Score: 251.06  E-value: 2.34e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    5 KVKVAVRIRPMNRRETDLHTKCVVDVDANKVIlnPVNTNLSKGDARGQPKV--FAYDHCFwsmDESVKekyagQDIVFKC 82
Cdd:cd01367    1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTL--IVHEPKLKVDLTKYIENhtFRFDYVF---DESSS-----NETVYRS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   83 LGENILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKV 158
Cdd:cd01367   71 TVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  159 RDLLDPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvK 238
Cdd:cd01367  150 FDLLNRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------R 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  239 SGTSGEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDS 317
Cdd:cd01367  220 DRGTNKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDS 293

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 46852172  318 L-GGNSKTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01367  294 FiGENSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
 6-351 6.94e-69

Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.


Pssm-ID: 276827 [Multi-domain]  Cd Length: 319  Bit Score: 235.09  E-value: 6.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    6 VKVAVRIRPMNRRETDLHTKCVVDvdankvILNPVNTNLSKGDARGQPKVFAYDHcFWSMDESVKEKYAGQdivFKClge 85
Cdd:cd01376    2 VRVAVRVRPFVDGTAGASDPSCVS------GIDSCSVELADPRNHGETLKYQFDA-FYGEESTQEDIYARE---VQP--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   86 nILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVEVSYMEIYNEKVRDLLDPK 165
Cdd:cd01376   69 -IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFTMSYLEIYQEKILDLLEPA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  166 GSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVksgTS 242
Cdd:cd01376  145 SKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---PF 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  243 GEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVPYRDSVLTWLLKDSLGGNS 322
Cdd:cd01376  217 RQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIPYRDSKLTRLLQDSLGGGS 290

                        330       340
                 ....*....|....*....|....*....
gi 46852172  323 KTAMVATVSPAADNYDETLSTLRYADRAK 351
Cdd:cd01376  291 RCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
 447-545 4.18e-68

forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438782 [Multi-domain]  Cd Length: 99  Bit Score: 224.02  E-value: 4.18e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22730    1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80

                         90
                 ....*....|....*....
gi 46852172  527 HHGDRILWGNNHFFRLNLP 545
Cdd:cd22730   81 HHGDRILWGNNHFFRINLP 99
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
 447-545 2.43e-59

forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 family includes KIF13A and KIF13B. KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. KIF13B, also called kinesin-like protein GAKIN, is a novel kinesin-like protein that associates with the human homolog of the Drosophila discs large tumor suppressor in T lymphocytes. It is involved in reorganization of the cortical cytoskeleton. It regulates axon formation by promoting the formation of extra axons. KIF13B may be functionally important for the intracellular trafficking of membrane-associated guanylate kinase homologs (MAGUKs) and associated protein complexes. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438758 [Multi-domain]  Cd Length: 101  Bit Score: 199.06  E-value: 2.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 523
Cdd:cd22706    1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79

                         90       100
                 ....*....|....*....|..
gi 46852172  524 IQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22706   80 TQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
 447-550 1.43e-55

forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called kinesin-like protein RBKIN, is a plus end-directed microtubule-dependent motor protein involved in intracellular transport and in regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis, and cytokinesis. It mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, KIF13A is required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. It is also required for the abscission step in cytokinesis: it mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438781 [Multi-domain]  Cd Length: 109  Bit Score: 188.56  E-value: 1.43e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  447 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 526
Cdd:cd22729    1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80

                         90       100
                 ....*....|....*....|....
gi 46852172  527 HHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22729   81 WHGDRILWGNNHFFRINLPKRKRR 104
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
 450-543 7.90e-34

forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 family includes KIF1A, KIF1B, and KIF1C. KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438757 [Multi-domain]  Cd Length: 101  Bit Score: 126.19  E-value: 7.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22705    4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82

                         90
                 ....*....|....*...
gi 46852172  526 LHHGDRILWGNNHFFRLN 543
Cdd:cd22705   83 LKTGSRVILGKNHVFRFN 100
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
 450-545 3.94e-31

forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; KIF14 is a microtubule motor protein that binds to microtubules with high affinity through each tubulin heterodimer and has an ATPase activity. It plays a role in many processes like cell division, cytokinesis and in cell proliferation and apoptosis. KIF14 is a potential oncogene and is involved in the metastasis of various cancers. Mutations of KIF14 cause primary microcephaly by impairing cytokinesis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438759 [Multi-domain]  Cd Length: 108  Bit Score: 118.52  E-value: 3.94e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22707   10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88

                         90       100
                 ....*....|....*....|
gi 46852172  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22707   89 LHHGDRVILGGDHYFRFNHP 108
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 1704-1767 3.26e-30

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 114.42  E-value: 3.26e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46852172   1704 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1767
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 448-545 1.57e-28

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 110.77  E-value: 1.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  448 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 522
Cdd:cd22709    1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79

                         90       100
                 ....*....|....*....|...
gi 46852172  523 PIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22709   80 ETELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 58-289 3.81e-28

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 112.44  E-value: 3.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   58 YDHCFWSMDeSVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQK 136
Cdd:cd01363   15 RDSKIIVFY-RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  137 EENEEQsfkvevsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMN 216
Cdd:cd01363   87 GETEGW-----------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRN 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852172  217 EESSRSHAVFKItlthtlydvksgtsgekvgklsLVDLAGSERatktgaagdrlkegsnINKSLTTLGLVISA 289
Cdd:cd01363  125 ENSSRFGKFIEI----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 1704-1768 5.92e-26

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 102.28  E-value: 5.92e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172    1704 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1768
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
357-469 7.11e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.38  E-value: 7.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    357 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 391
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172    392 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 454
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160

                          170
                   ....*....|....*
gi 46852172    455 ADPALNELLVYYLKE 469
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
 450-547 1.63e-23

forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, is a motor for anterograde transport of mitochondria. It has a microtubule plus end-directed motility. Isoform 1 mediates the transport of synaptic vesicles in neuronal cells, while isoform 2 is required for induction of neuronal apoptosis. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438779 [Multi-domain]  Cd Length: 110  Bit Score: 97.03  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 521
Cdd:cd22727    5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84

                         90       100
                 ....*....|....*....|....*.
gi 46852172  522 SPIQLHHGDRILWGNNHFFRLNLPKK 547
Cdd:cd22727   85 QPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
 450-554 4.83e-20

forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called axonal transporter of synaptic vesicles (ATSV), microtubule-based motor KIF1A, Unc-104- and KIF1A-related protein, or Unc-104, is an axonal transporter of synaptic vesicles, which is mutated in hereditary sensory and autonomic neuropathy type 2. It is also required for neuronal dense core vesicle (DCV) transport to dendritic spines and axons. The calcium-dependent interaction with CALM1 increases vesicle motility, and interaction with the scaffolding proteins PPFIA2 and TANC2 recruits DCVs to synaptic sites. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438778 [Multi-domain]  Cd Length: 115  Bit Score: 87.29  E-value: 4.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 521
Cdd:cd22726    4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 46852172  522 SPIQLHHGDRILWGNNHFFRLNLPKKKKKaERE 554
Cdd:cd22726   84 EPSILRSGNRIIMGKSHVFRFNHPEQARQ-ERE 115
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
 5-162 3.73e-19

Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 85.73  E-value: 3.73e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172      5 KVKVAVRIRPMNRREtdlhtkcvvdvdankVILNPVNTNLSKGDARGQPKVFAYDHCFwsmdesvkEKYAGQDIVFKCLg 84
Cdd:pfam16796   21 NIRVFARVRPELLSE---------------AQIDYPDETSSDGKIGSKNKSFSFDRVF--------PPESEQEDVFQEI- 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172     85 ENILQNAFDGYNACIFAYGQTGSGKSytmmgtadqPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 162
Cdd:pfam16796   77 SQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWK-YTIELQFVEIYNESSQDLL 144
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
 450-543 1.72e-17

forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. It has a microtubule plus end-directed motility. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438780 [Multi-domain]  Cd Length: 102  Bit Score: 79.53  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 524
Cdd:cd22728    4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82

                         90
                 ....*....|....*....
gi 46852172  525 QLHHGDRILWGNNHFFRLN 543
Cdd:cd22728   83 VLKSGNRIVMGKNHVFRFN 101
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
 450-545 3.87e-17

forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 family includes StARD9/KIF16A and KIF16B. StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438760 [Multi-domain]  Cd Length: 109  Bit Score: 78.85  E-value: 3.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22708   11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89

                         90       100
                 ....*....|....*....|
gi 46852172  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22708   90 LTQGDVILLGKTNMFRFNHP 109
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
 448-545 2.80e-15

forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ALL1-fused gene from chromosome 6 protein, protein AF-6, Afadin adherens junction formation factor, or MLLT4, is a nectin- and actin-filament-binding protein that connects nectin to the actin cytoskeleton. It is essential for the organization of adherens junctions. It may play a key role in the organization of epithelial structures of the embryonic ectoderm. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438763 [Multi-domain]  Cd Length: 106  Bit Score: 73.51  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  448 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 515
Cdd:cd22711    2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76

                         90       100       110
                 ....*....|....*....|....*....|
gi 46852172  516 NGSSVSSPIQLHHGDRILWGNNHFFRLNLP 545
Cdd:cd22711   77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 468-539 1.19e-13

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 68.39  E-value: 1.19e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852172  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTP-QKNTRTFVNGSSVSSPIQLHHGDRILWGNNHF 539
Cdd:cd22673   20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
 756-802 1.95e-13

Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00225, pfam00498. KIF1B is an anterograde motor for transport of mitochondria in axons of neuronal cells.


Pssm-ID: 463574  Cd Length: 43  Bit Score: 66.09  E-value: 1.95e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172    756 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 802
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
 438-549 2.37e-13

forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 (PHLDB1) and similar proteins; PHLDB1, also called protein LL5-alpha (LL5A), acts as an insulin-responsive protein that enhances Akt activation. PHLDB1 contains a pleckstrin homology domain, which binds phosphatidylinositol PI(3,4)P(2), PI(3,5)P(2), and PI(3,4,5)P(3), as well as a Forkhead-associated (FHA) domain and coiled coil regions. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438765  Cd Length: 120  Bit Score: 68.12  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  438 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 516
Cdd:cd22713    7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 46852172  517 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 549
Cdd:cd22713   85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 1704-1773 4.52e-13

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 74.34  E-value: 4.52e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1704 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1773
Cdd:COG5244    7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
 450-550 1.72e-12

forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called sorting nexin-23, is a plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. It regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). It regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438784 [Multi-domain]  Cd Length: 117  Bit Score: 65.73  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22732   11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89

                         90       100
                 ....*....|....*....|....*
gi 46852172  526 LHHGDRILWGNNHFFRLNLPKKKKK 550
Cdd:cd22732   90 LNQGAVILLGRTNMFRFNHPKEAAK 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1424-1683 1.28e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 70.35  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1492
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1493 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1569
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1570 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1641
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 46852172  1642 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1683
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 471-534 3.70e-11

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 60.28  E-value: 3.70e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46852172    471 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 534
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 449-539 5.18e-11

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 60.75  E-value: 5.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  449 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 527
Cdd:cd00060    1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77

                         90
                 ....*....|..
gi 46852172  528 HGDRILWGNNHF 539
Cdd:cd00060   78 DGDVIRLGDTTF 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1421-1699 5.49e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.43  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1421 RGIAPAPAL-SVSPQNNHSPDP---GLSNLAASYLNPVKSFVPQMPKLLKSLFP--VRDEKRGKRPS--PLAHQPVPRIM 1492
Cdd:PHA03247 2605 RGDPRGPAPpSPLPPDTHAPDPpppSPSPAANEPDPHPPPTVPPPERPRDDPAPgrVSRPRRARRLGraAQASSPPQRPR 2684

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1493 VQSASPDI-RVTRM-----EEAQPEMGPDVLVQTMGAP-----ALKICDKPAKVPSPPPVIAVTAV------TPAPEAQD 1555
Cdd:PHA03247 2685 RRAARPTVgSLTSLadpppPPPTPEPAPHALVSATPLPpgpaaARQASPALPAAPAPPAVPAGPATpggparPARPPTTA 2764

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1556 GPPSPLSEAS-----------SGYFSHSVSTATLSDALGP--------GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV 1616
Cdd:PHA03247 2765 GPPAPAPPAApaagpprrltrPAVASLSESRESLPSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1617 PAEEPPGPQQLVSPG---RERPDLEAPA--PGSPFR--VRRVRASELRSFSRMLAGDPgcsPGAEgNAPAPGAGGQALAS 1689
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGgdvRRRPPSRSPAakPAAPARppVRRLARPAVSRSTESFALPP---DQPE-RPPQPQAPPPPQPQ 2920

                         330
                  ....*....|
gi 46852172  1690 DSEEADEVPE 1699
Cdd:PHA03247 2921 PQPPPPPQPQ 2930
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
 450-545 3.57e-10

forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); StARD9, also called START domain-containing protein 9, or kinesin-like protein KIF16A, is a microtubule-dependent motor protein required for spindle pole assembly during mitosis. It is required to stabilize the pericentriolar material (PCM). The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438783 [Multi-domain]  Cd Length: 119  Bit Score: 59.40  E-value: 3.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  450 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 525
Cdd:cd22731   11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89

                         90       100
                 ....*....|....*....|
gi 46852172  526 LHHGDRILWGNNHFFRLNLP 545
Cdd:cd22731   90 LSQGAVIVLGKTHKFRFNHP 109
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
 446-540 1.01e-09

forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing protein (Radil)-like family; The Radil-like family includes Radil and Ras-interacting protein 1 (Rain). Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility by linking Rap1 to beta2-integrin activation. Rain, also called Rasip1, is an endothelial-specific Ras-interacting protein required for the proper formation of vascular structures that develop via both vasculogenesis and angiogenesis. It acts as a critical and vascular-specific regulator of GTPase signaling, cell architecture, and adhesion, which is essential for endothelial cell morphogenesis and blood vessel tubulogenesis. Rain interacts with Ras in a GTP-dependent manner and may serve as an effector for endomembrane-associated Ras. Both Radil and Rain contain an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438764 [Multi-domain]  Cd Length: 120  Bit Score: 58.08  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  446 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 506
Cdd:cd22712    2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 46852172  507 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 540
Cdd:cd22712   82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1536-1694 2.15e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 62.88  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1536 PSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA 1615
Cdd:PHA03307  114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1616 V----PAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRmlagDPGCSPGAEGNAPAPGAGGQALASDS 1691
Cdd:PHA03307  194 PpstpPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE----SSGCGWGPENECPLPRPAPITLPTRI 269


                  ...
gi 46852172  1692 EEA 1694
Cdd:PHA03307  270 WEA 272
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1538-1681 2.97e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.65  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1538 PPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfSHSVSTATLSDA-------LGPGLDAAAPPGSMPTAPeAEPEAPISHP 1610
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSE---PAVTSRARRPDAppqsarpRAPVDDRGDPRGPAPPSP-LPPDTHAPDP 2626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1611 PPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPGAEGNAPAPG 1681
Cdd:PHA03247 2627 PPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLTSLADPPPPP 2705
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1508-1682 1.26e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 59.89  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1508 AQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIA-VTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGL 1586
Cdd:PRK12323  375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPaAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP 454

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1587 DAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRASELRSFSRMLAGD 1666
Cdd:PRK12323  455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWVAESIPDPATAD 533

                         170
                  ....*....|....*.
gi 46852172  1667 PgcSPGAEGNAPAPGA 1682
Cdd:PRK12323  534 P--DDAFETLAPAPAA 547
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 1532-1655 1.77e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 59.34  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1532 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGyfshsvstatlsdalgpglDAAAPPGSMPTAPEAEPEAPISHPP 1611
Cdd:PRK14951  389 PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA-------------------PVAAPAAAAPAAAPAAAPAAVALAP 449

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 46852172  1612 PPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASE 1655
Cdd:PRK14951  450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1480-1650 1.93e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1480 PSPLAHQPVPrimvQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1559
Cdd:PRK07764  636 PAEASAAPAP----GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA---APPPAPAPAAPAAPAGAAPAQPAPAPAAT 708

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1560 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1639
Cdd:PRK07764  709 PPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788

                         170
                  ....*....|.
gi 46852172  1640 PAPGSPFRVRR 1650
Cdd:PRK07764  789 DAPSMDDEDRR 799
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1480-1799 2.17e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 59.41  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1480 PSPLAHQPV---PRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDG 1556
Cdd:PHA03307   28 PGDAADDLLsgsQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1557 PPSPLSEASSGYFSHSVS------TATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA------VPAEEPPGP 1624
Cdd:PHA03307  108 PPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAalplssPEETARAPS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1625 qqlvSPGRERPDLEAPAPGSPfrvrrvRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREG 1704
Cdd:PHA03307  188 ----SPPAEPPPSTPPAAASP------RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1705 EFVTVGAHKTGVVRYVGpadfqegtWVGVELDLPSGKNDGSIGGK--QYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLR 1782
Cdd:PHA03307  258 PRPAPITLPTRIWEASG--------WNGPSSRPGPASSSSSPRERspSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329

                         330
                  ....*....|....*..
gi 46852172  1783 LGAPEARRSATLSGSAT 1799
Cdd:PHA03307  330 SSSSESSRGAAVSPGPS 346
PHA03378 PHA03378
EBNA-3B; Provisional
 1371-1686 3.22e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 58.93  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1371 GKGKLSRRSISSPNVNRLSGSrqdlIPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASY 1450
Cdd:PHA03378  568 GLGPLQIQPLTSPTTSQLASS----APSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPITF 643

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1451 LNPVKSFVPQMPKLLKSLFPVRDEKRGKRPsplaHQPVPRIMVQSASPDIRVTRMEEaqPEMGPDVLVQTMGAPALKICD 1530
Cdd:PHA03378  644 NVLVFPTPHQPPQVEITPYKPTWTQIGHIP----YQPSPTGANTMLPIQWAPGTMQP--PPRAPTPMRPPAAPPGRAQRP 717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1531 KPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP 1610
Cdd:PHA03378  718 AAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46852172  1611 PPPTAVPAEEPPGPQQLvsPGRERPDLEAPAPGSPFRVRRVRASeLRSFSRmlagdpGCSPGAEGNAPAPGAGGQA 1686
Cdd:PHA03378  798 PPPQAGPTSMQLMPRAA--PGQQGPTKQILRQLLTGGVKRGRPS-LKKPAA------LERQAAAGPTPSPGSGTSD 864
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1523-1699 4.69e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.07  E-value: 4.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1523 APALKICDKPAKVPSPPPViAVTAVTPAPEAQDGPPSPLSEASSGYFSHS--------VSTATLSDALGPGLDAAAPPGS 1594
Cdd:PRK07764  602 APASSGPPEEAARPAAPAA-PAAPAAPAPAGAAAAPAEASAAPAPGVAAPehhpkhvaVPDASDGGDGWPAKAGGAAPAA 680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1595 MPTAPEAEPEAPISHPPPPTAVPAE--EPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPG 1672
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPaaTPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                         170       180
                  ....*....|....*....|....*..
gi 46852172  1673 AEGNAPAPGAGGQALASDSEEADEVPE 1699
Cdd:PRK07764  761 PPAPAPAAAPAAAPPPSPPSEEEEMAE 787
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
79-290 5.82e-08

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 57.83  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   79 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 156
Cdd:COG5059  370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  157 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 235
Cdd:COG5059  442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 46852172  236 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 290
Cdd:COG5059  511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 1439-1753 5.85e-08

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.77  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1439 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1518
Cdd:COG5180  174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1519 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1593
Cdd:COG5180  253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1594 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1657
Cdd:COG5180  332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1658 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1735
Cdd:COG5180  412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484

                        330
                 ....*....|....*...
gi 46852172 1736 DLPSGKNDGSIGGKQYFR 1753
Cdd:COG5180  485 LGVRPDAILGGNVAPASG 502
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1425-1730 9.01e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.49  E-value: 9.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1425 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTR 1504
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSS-----PISASASSPAPAPGRSAADDAGASSSDSSSSESSG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1505 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEaqDGPPSPLSEASSGyfshSVSTATLSDALGP 1584
Cdd:PHA03307  247 CGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER--SPSPSPSSPGSGP----APSSPRASSSSSS 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1585 ----GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfRVRRVRASELRSFS 1660
Cdd:PHA03307  321 sresSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP-TRRRARAAVAGRAR 399

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852172  1661 RMLAgdPGCSPGAEGNAPAPGAGGQALASDSEEADEVPewlrEGE-FVTVGAHKTGVVRYVGPADFQEGTW 1730
Cdd:PHA03307  400 RRDA--TGRFPAGRPRPSPLDAGAASGAFYARYPLLTP----SGEpWPGSPPPPPGRVRYGGLGDSRPGLW 464
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 1476-1655 1.86e-07

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 55.56  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1476 RGKRPSPLAHQP-----VPRIMVQSASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI------- 1542
Cdd:pfam13254  165 KPKAQPSQPAQPawmkeLNKIRQSRASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeep 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1543 AVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPP 1622
Cdd:pfam13254  238 SEEADTLSTDKEQSPAPTSASEPPPKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKAS 315

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 46852172   1623 GPQQLVSPGRErPDLEAPAPGSP---FRV---RRVRASE 1655
Cdd:pfam13254  316 IDKPLSSPDRD-PLSPKPKPQSPpkdFRAnlrSREVPKD 353
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1490-1632 4.71e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.99  E-value: 4.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1490 RIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP-PSPLSE 1563
Cdd:PRK07764  361 RMLLPSASDDErgllaRLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPaPAPAPA 440

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852172  1564 ASSGYFSHSVSTATLSDalgPGLDAAAPPGSMPTAPE----AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR 1632
Cdd:PRK07764  441 PPSPAGNAPAGGAPSPP---PAAAPSAQPAPAPAAAPeptaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
 1221-1278 7.82e-07

Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and 151 amino acids in length. The family is found in association with pfam00225, pfam00498. There is a single completely conserved residue W that may be functionally important.


Pssm-ID: 463599  Cd Length: 149  Bit Score: 50.28  E-value: 7.82e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46852172   1221 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1278
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 1469-1642 8.21e-07

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 52.30  E-value: 8.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1469 FPVRDEKRGKRP----------SPLAHQPVPRIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPA 1533
Cdd:pfam15822   16 SAVSNPKPGQPPqgwpgsnpwnNPSAPPAVPSGLPPSTAPSTvpfgpAPTGMYPSIPLTGPSPGPPAPFPPSGPSCPPPG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1534 KvPSPPPVIAvtavTPAPEAQDGPPS-PLSEASSGYFSHS--VSTATL-------SDALGPGLDAAAPPGSMPTAPeaep 1603
Cdd:pfam15822   96 G-PYPAPTVP----GPGPIGPYPTPNmPFPELPRPYGAPTdpAAAAPSgpwgsmsSGPWAPGMGGQYPAPNMPYPS---- 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 46852172   1604 eaPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAP 1642
Cdd:pfam15822  167 --PGPYPaVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDP 204
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1396-1642 1.00e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.00  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1396 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1475
Cdd:pfam03154  148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1476 rgkrpSPLAhqpvPRIMVQSaSPDIRVTRMEEAQPEMGPdvlvQTMGAPALKICDKPakvpSPPPVIAvTAVTPAPEA-Q 1554
Cdd:pfam03154  223 -----STAA----PHTLIQQ-TPTLHPQRLPSPHPPLQP----MTQPPPPSQVSPQP----LPQPSLH-GQMPPMPHSlQ 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1555 DGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ-- 1625
Cdd:pfam03154  284 TGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpi 363

                          250       260
                   ....*....|....*....|
gi 46852172   1626 -QLVSPGRER--PDLEAPAP 1642
Cdd:pfam03154  364 pQLPNPQSHKhpPHLSGPSP 383
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1424-1621 1.97e-06

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 52.85  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1424 APAPALSVSPQNNhSPDPGLSNlAASYLNPVKSFVP---QMPKLLK---SLFPVRDEKRGKRPSplAHQPVPRIMVQSas 1497
Cdd:pfam03154  348 APLSMPHIKPPPT-TPIPQLPN-PQSHKHPPHLSGPspfQMNSNLPpppALKPLSSLSTHHPPS--AHPPPLQLMPQS-- 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1498 pdirvtrMEEAQPEMGPDVLVQTMGAPALKICDKPA----KVPSPPPVIA---VTAVTPAPEAQDGPPSPLSEASSGYFS 1570
Cdd:pfam03154  422 -------QQLPPPPAQPPVLTQSQSLPPPAASHPPTsglhQVPSQSPFPQhpfVPGGPPPITPPSGPPTSTSSAMPGIQP 494

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 46852172   1571 HSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPIShPPPPTAVPAEEP 1621
Cdd:pfam03154  495 PSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPES-PPPPPRSPSPEP 544
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1414-1686 3.69e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1414 VSQTTVSRGIAPAP-ALSVSPQNNHSPDPGLSNLA--ASYLNPVKSFVPQMPKLLKSLFPVRDEKRG---------KRPS 1481
Cdd:PHA03247 2788 VASLSESRESLPSPwDPADPPAAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPP 2867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1482 PLAHQPVPrimvqSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAV-TPAPEAQDGPPSP 1560
Cdd:PHA03247 2868 SRSPAAKP-----AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPP 2942

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1561 LS----EASSGYFSHSVSTATLSdALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPA-----------EEP-PGP 1624
Cdd:PHA03247 2943 LApttdPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslalhEETdPPP 3021

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1625 ----QQLVSPGR--------------ERPDLEAPAPgspfrvrrvraselrsfsrmLAGDPGCSPGAEGNAPAPGAGGQA 1686
Cdd:PHA03247 3022 vslkQTLWPPDDtedsdadslfdsdsERSDLEALDP--------------------LPPEPHDPFAHEPDPATPEAGARE 3081
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1422-1698 3.88e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1422 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqsASPDI 1500
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPP------AAPDR 2566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1501 RVTRMEEAQPEMGPDVLVQTM--GAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATL 1578
Cdd:PHA03247 2567 SVPPPRPAPRPSEPAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTV 2646

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1579 SDALGPGLDAAAPPGSM---------PTAPEAEPEAP--------------ISHPPPPTAVPAEEP-------PGPQQLV 1628
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRprrarrlgrAAQASSPPQRPrrraarptvgsltsLADPPPPPPTPEPAPhalvsatPLPPGPA 2726

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46852172  1629 SPGRERPDLE-APAPGSPFRVRRVRASELRSFSRMLAGDPGCS--PGAEGNAPAPGAGGQALASDSEEADEVP 1698
Cdd:PHA03247 2727 AARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLP 2799
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1537-1699 4.14e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1537 SPPPVIAVTAVTPAPEAQdgPPSPLSEASSGYFSHSVSTATLSDALGPgldAAAPPGSMPTAPEAEPEA-------PISH 1609
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAA--APAAAAPAPAAPPAAPAAAPAAAAAARA---VAAAPARRSPAPEALAAArqasargPGGA 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1610 PPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVR-RVRASELRSFSRMLAGDPGcSPGAEGNAPAPGAGGQALA 1688
Cdd:PRK12323  448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAaPAPADDDPPPWEELPPEFA-SPAPAQPDAAPAGWVAESI 526

                         170
                  ....*....|.
gi 46852172  1689 SDSEEADEVPE 1699
Cdd:PRK12323  527 PDPATADPDDA 537
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1477-1695 8.45e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.64  E-value: 8.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1477 GKRPSPLAHQPVPRIMVQSASPdirvtrmEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPViAVTAVTPAPEAQDG 1556
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAP-------AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSP-APEALAAARQASAR 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1557 PPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEP-PGPQQL-------- 1627
Cdd:PRK12323  443 GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFAsPAPAQPdaapagwv 522

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1628 ---------VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAG------GQALASDSE 1692
Cdd:PRK12323  523 aesipdpatADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARlpvrglAQQLARQSE 602


                  ...
gi 46852172  1693 EAD 1695
Cdd:PRK12323  603 LAG 605
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1533-1654 8.68e-06

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 50.15  E-value: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1533 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1604
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46852172  1605 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1654
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1572-1680 9.37e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1572 SVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP----------------------PPPTAVPAEEPPGPQQLVS 1629
Cdd:PHA03247 2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPvhprmltwirgleelasddagdPPPPLPPAAPPAAPDRSVP 2569

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 46852172  1630 PGRERPDLEAPAPGSpfRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAP 1680
Cdd:PHA03247 2570 PPRPAPRPSEPAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1573-1731 1.07e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1573 VSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVR 1652
Cdd:PRK07764  393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1653 ASEL--RSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAhktgVVRYVGPADFQEGTW 1730
Cdd:PRK07764  473 APEPtaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI----LLPEATVLGVRGDTL 548


                  .
gi 46852172  1731 V 1731
Cdd:PRK07764  549 V 549
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
468-542 1.14e-05

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 45.72  E-value: 1.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172  468 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 542
Cdd:COG1716   20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 1520-1621 1.29e-05

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 49.15  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1520 TMGAPALKICDkPAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseassgyfshsvsTATLSDALGPGldaAAPPGSMPTAP 1599
Cdd:pfam07174   30 AVALPAVAHAD-PEPAPPPPSTATAPPAPPPPPPAPAAPAP--------------PPPPAAPNAPN---APPPPADPNAP 91

                           90       100
                   ....*....|....*....|..
gi 46852172   1600 EAEPEAPISHPPPPTAVPAEEP 1621
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNAPEP 113
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1494-1646 1.30e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 50.15  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1494 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV 1573
Cdd:pfam03154  142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP-----TPSAPSVPPQGSPATSQ 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1574 STATLSDALGP-GLDAAAPPGSMPTAPEAEPE-APISHPPPPTAVPAEE----------PPGPQQLVS-PgrerPDLEAP 1640
Cdd:pfam03154  217 PPNQTQSTAAPhTLIQQTPTLHPQRLPSPHPPlQPMTQPPPPSQVSPQPlpqpslhgqmPPMPHSLQTgP----SHMQHP 292


                   ....*.
gi 46852172   1641 APGSPF 1646
Cdd:pfam03154  293 VPPQPF 298
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 1389-1645 2.24e-05

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteriztic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 48.66  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1389 SGSRQDLI-PSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLaasylNPVKSFVPQMPKLLKS 1467
Cdd:pfam15279   62 AGSSAQLItPDLWLSDCRRKSASPASTRSESVSPGPSSSASPSSSPTSSNSSKPLISVA-----SSSKLLAPKPHEPPSL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1468 LFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPV----IA 1543
Cdd:pfam15279  137 PPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAFMEPSSMP---PPFLRPPPSIPqpnsPL 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1544 VTAVTPAPEAQDGPPSPLSEASSGY----FS--HSVSTATLSdalGPgldaaaPPGSMPTAPEAEPeaPISHPPPPtavP 1617
Cdd:pfam15279  214 SNPMLPGIGPPPKPPRNLGPPSNPMhrppFSphHPPPPPTPP---GP------PPGLPPPPPRGFT--PPFGPPFP---P 279

                          250       260
                   ....*....|....*....|....*...
gi 46852172   1618 AEEPPGPQQLvspgreRPDLEAPAPGSP 1645
Cdd:pfam15279  280 VNMMPNPPEM------NFGLPSLAPLVP 301
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1508-1690 2.87e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1508 AQPEMGPdVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLD 1587
Cdd:PRK07003  395 AVPAVTA-VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPAD 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1588 A---AAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQqlvspGRERPDleAPAPGSPfrvrrvraselrsfsrmla 1664
Cdd:PRK07003  474 SgsaSAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-----AASRED--APAAAAP------------------- 527

                         170       180       190
                  ....*....|....*....|....*....|...
gi 46852172  1665 gdpgcsPGAEGNAPAPGA-------GGQALASD 1690
Cdd:PRK07003  528 ------PAPEARPPTPAAaapaaraGGAAAALD 554
PHA03377 PHA03377
EBNA-3C; Provisional
 1450-1643 2.90e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 49.28  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1450 YLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDirvtRMEEAQ--PEM-GP-DVLVQTMGAPA 1525
Cdd:PHA03377  392 YIDPNMEPVQQRPVMFVSRVPWRKPRTLPWPTPKTHPVKRTLVKTSGRSD----EAEQAQstPERpGPsDQPSVPVEPAH 467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1526 LKICDKP-AKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV-------STATLSDALGPGLDAAAP------ 1591
Cdd:PHA03377  468 LTPVEHTtVILHQPPQSPPTVAIKPAP-----PPSRRRRGACVVYDDDIievidveTTEEEESVTQPAKPHRKVqdgfqr 542

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46852172  1592 PGSMPTAPEAEPEAPISHPPPPTAVPAEEPP--GPQQLVSPGRERPDLEAPAPG 1643
Cdd:PHA03377  543 SGRRQKRATPPKVSPSDRGPPKASPPVMAPPstGPRVMATPSTGPRDMAPPSTG 596
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 1532-1645 3.72e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 45.63  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1532 PAKVPSPPPVIAVTAVTPAP----EAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPI 1607
Cdd:pfam06346   18 GACIPTPPPLPGGGGPPPPPplpgSAAIPPPPPL----------------------PGGTSIPPPPPLPGAASIPPPPPL 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172   1608 SH----PPPP-----TAVPAEEPPGPQqlvSPGRERPdlEAPAPGSP 1645
Cdd:pfam06346   76 PGstgiPPPPplpggAGIPPPPPPLPG---GAGVPPP--PPPLPGGP 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1535-1698 4.54e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 4.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1535 VPSPPPVIAVTAVTPaPEAQDG--PPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPISHPPP 1612
Cdd:PHA03247  254 APAPPPVVGEGADRA-PETARGatGPPPPPEAAA-----------------PNGAAAPPDGVWGAALAGAPLALPAPPDP 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1613 PTAVPAEEP----------------PGPQQLVS---PGRERP---------DLEA---PAPGSPFRVRRVRASELRS--F 1659
Cdd:PHA03247  316 PPPAPAGDAeeeddedgamevvsplPRPRQHYPlgfPKRRRPtwtppssleDLSAgrhHPKRASLPTRKRRSARHAAtpF 395

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 46852172  1660 SRMLAGD--PGCSPGAEGNAPAPGAGGQALASDSEEADEVP 1698
Cdd:PHA03247  396 ARGPGGDdqTRPAAPVPASVPTPAPTPVPASAPPPPATPLP 436
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1541-1698 5.15e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 5.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1541 VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEE 1620
Cdd:PRK07764  584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172  1621 PPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADEVP 1698
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--AGQADDPAAQPPQAAQGASAPSPAADDPV 739
PHA03369 PHA03369
capsid maturational protease; Provisional
 1410-1643 7.04e-05

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 47.69  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1410 SQQDVSQTTVSRGI--APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLF------PVRDEKRGKRPS 1481
Cdd:PHA03369  393 SVPARSPMTAYPPVpqFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPISMANMVypghpqEHGHERKRKRGG 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1482 PL------AHQPVPRIMVQ---SASPDIRVTRMEEAQPEM---GPDVLVQTMGAPALKICDKPA-----KVPSPPPVIAV 1544
Cdd:PHA03369  473 ELkeelieTLKLVKKLKEEqesLAKELEATAHKSEIKKIAeseFKNAGAKTAAANIEPNCSADAaapatKRARPETKTEL 552

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1545 TAVTPAPEAQDGPPSPLseassgyFSHSVSTATLSDALGPGLDAAA----------------PPGSMPTAPEAEPEAPIS 1608
Cdd:PHA03369  553 EAVVRFPYQIRNMESPA-------FVHSFTSTTLAAAAGQGSDTAEalagaietlltqasaqPAGLSLPAPAVPVNASTP 625

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 46852172  1609 HPPPPTAVPAEEPPgpqqlvsPGRERPDLEAPAPG 1643
Cdd:PHA03369  626 ASTPPPLAPQEPPQ-------PGTSAPSLETSLPQ 653
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 1531-1695 8.26e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.40  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1531 KP-AKVPSPPPVIAVTAVTPAPEAQDgpPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPish 1609
Cdd:PRK14951  365 KPaAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAA-----------------APAPAAAPAAAASAPAAPPAAAP--- 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1610 pPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvrrvrasELRSFSRMLAGDPGCSPGAEGNAPAPGAggqALAS 1689
Cdd:PRK14951  423 -PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP---------ETVAIPVRVAPEPAVASAAPAPAAAPAA---ARLT 489


                  ....*.
gi 46852172  1690 DSEEAD 1695
Cdd:PRK14951  490 PTEEGD 495
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
 1099-1143 1.31e-04

Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact specifically with GTP-bound Rab proteins and mediate their versatile roles in membrane trafficking, including budding of vesicles from a donor membrane, directed transport through the cell and finally tethering and fusion with a target membrane. The 'bivalent Mical/EHBP Rab binding' (bMERB) domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. The bMERB domain displays a preference for Rab8 family proteins (Rab8, 10, 13 and 15) and at least some of the bMERB domains contain two separate binding sites for Rab-proteins, allowing Micals and EHBPs to bind two Rabs simultaneously. The strong similarity between the two binding sites within one bMRB domain strongly suggests an evolutionarily development via duplication of a common ancestor supersecondary structure element. The bMERB domain has a completely alpha-helical fold consisting of a central helix and N- and C-terminal helices folding back on this central helix.


Pssm-ID: 463467 [Multi-domain]  Cd Length: 131  Bit Score: 43.66  E-value: 1.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 46852172   1099 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1143
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1424-1645 2.63e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 45.92  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1503
Cdd:NF033839  294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1504 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1582
Cdd:NF033839  356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172  1583 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1645
Cdd:NF033839  411 -PQPEKPKPevkPQPEKPKPEVKPQ-----PEKPKPEVKPQPEKPKPEVKPQPETPKPEVkPQPEKP 471
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1479-1700 3.00e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1479 RPSPLAhqpvPRIMVQSASPDIRVTRM---EEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqD 1555
Cdd:PRK07003  411 APKAAA----AAAATRAEAPPAAPAPPataDRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS---D 483

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1556 GPPSPLSEASSgyfshsvSTATLSDALGPGLDAAAPPGSMPTAPEAEPEA-PISHPPPPTavPAEEPPGPQQ-------- 1626
Cdd:PRK07003  484 APPDAAFEPAP-------RAAAPSAATPAAVPDARAPAAASREDAPAAAApPAPEARPPT--PAAAAPAARAggaaaald 554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1627 -------LVSPGRERPDLEAPAPGSPfrvrrVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADE-VP 1698
Cdd:PRK07003  555 vlrnagmRVSSDRGARAAAAAKPAAA-----PAAAPKPAAPRVAVQVP--TPRARAATGDAPPNGAARAEQAAESRGaPP 627


                  ..
gi 46852172  1699 EW 1700
Cdd:PRK07003  628 PW 629
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 1533-1698 3.40e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 45.30  E-value: 3.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1533 AKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfshSVSTATLSDALGPgldaaaPPGSMPTAPEAEPEAP------ 1606
Cdd:PLN03209  336 ADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPR-----PLSPYTAYEDLKP------PTSPIPTPPSSSPASSksvdav 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1607 --------ISHPPPPTAVPAEEP-PGPQQL---VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAE 1674
Cdd:PLN03209  405 akpaepdvVPSPGSASNVPEVEPaQVEAKKtrpLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAAT 484

                         170       180
                  ....*....|....*....|....
gi 46852172  1675 GNAPAPGAGGQALASDSEEADEVP 1698
Cdd:PLN03209  485 DAAAPPPANMRPLSPYAVYDDLKP 508
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1532-1684 3.79e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.20  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1532 PAKVPSPPPviavtavTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAP----------PGSMP--- 1596
Cdd:PRK14086   90 PSAGEPAPP-------PPHARRTSEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPaypayqqrpePGAWPraa 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1597 ------------------TAPEAEPEAPISHPPPPTAVPAEEPPGPQQ-------LVSPGRERPDLEAPAPGSPFRVRRV 1651
Cdd:PRK14086  163 ddygwqqqrlgfpprapyASPASYAPEQERDREPYDAGRPEYDQRRRDydhprpdWDRPRRDRTDRPEPPPGAGHVHRGG 242

                         170       180       190
                  ....*....|....*....|....*....|....
gi 46852172  1652 R-ASELRSFSRMLAGDPGCSPGAEGNAPAPGAGG 1684
Cdd:PRK14086  243 PgPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
 1505-1641 4.14e-04

Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like transcription factors (KLFs) belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the related N-terminal domains of KLF9, KLF13, KLF14, KLF16, and similar proteins.


Pssm-ID: 409240 [Multi-domain]  Cd Length: 163  Bit Score: 42.76  E-value: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1505 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1573
Cdd:cd21975   12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46852172 1574 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1641
Cdd:cd21975   88 SLESGDADMGSDSDVAPASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1523-1698 5.16e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.84  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1523 APALKICDKPAKVPSPPPVIAVtavtPAPEAQdgpPSPLSEASSGYFSHSVSTATLSdalgpgldAAAPPGSMPTAPeAE 1602
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAV----PAPGAR---AAAAVGASAVPAVTAVTGAAGA--------ALAPKAAAAAAA-TR 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1603 PEAPISHPPPPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGA 1682
Cdd:PRK07003  423 AEAPPAAPAPPATADRGDDAADGDAPVPA------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496

                         170
                  ....*....|....*.
gi 46852172  1683 GGQALASDSEEADEVP 1698
Cdd:PRK07003  497 AAPSAATPAAVPDARA 512
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1424-1642 5.47e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1424 APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqSASPdIRVT 1503
Cdd:PRK12323  389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP-----AAAP-AAAA 462

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1504 RMEEAQPEmgpdvlvqtmGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALG 1583
Cdd:PRK12323  463 RPAAAGPR----------PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 46852172  1584 PGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlVSPGrERPDLEAPAP 1642
Cdd:PRK12323  533 DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD-MFDG-DWPALAARLP 589
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1476-1647 5.65e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.16  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1476 RGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPalkiCDKPAKVPSPPPVIAVTAVTPAPEAQD 1555
Cdd:PHA03307  764 VPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAA----SRTASKRKSRSHTPDGGSESSGPARPP 839

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1556 GP-PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgreR 1634
Cdd:PHA03307  840 GAaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP---M 916

                         170
                  ....*....|...
gi 46852172  1635 PdLEAPAPGSPFR 1647
Cdd:PHA03307  917 P-PGGPDPRGGFR 928
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 1543-1642 7.18e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 43.76  E-value: 7.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1543 AVTAVTPAPEAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPgsMPTAPEAEPEAPISHPPPPTAVPAEEPP 1622
Cdd:pfam07174   28 AVAVALPAVAHADPEPAPP----------------------PPSTATAPP--APPPPPPAPAAPAPPPPPAAPNAPNAPP 83

                           90       100
                   ....*....|....*....|
gi 46852172   1623 GPQQLVSPGRERPDLEAPAP 1642
Cdd:pfam07174   84 PPADPNAPPPPPADPNAPPP 103
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 1579-1663 7.91e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.22  E-value: 7.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1579 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1655
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101


                  ....*...
gi 46852172  1656 LRSFSRML 1663
Cdd:NF041121  102 PLELARAL 109
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
 460-540 9.21e-04

forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein (Radil); Radil acts as an important small GTPase Rap1 effector required for cell spreading and migration. It regulates neutrophil adhesion and motility through linking Rap1 to beta2-integrin activation. It contains an FHA domain. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438785  Cd Length: 113  Bit Score: 40.55  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  460 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 529
Cdd:cd22733   18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97

                         90
                 ....*....|.
gi 46852172  530 DRILWGNNHFF 540
Cdd:cd22733   98 DLLSFGAYYLF 108
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1480-1641 1.06e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1480 PSPLAHQPVPRImvqSASPDIRVTRMEEAQPEmGPDVLVQTMGAPAlkicdkPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1559
Cdd:PRK07764  651 EHHPKHVAVPDA---SDGGDGWPAKAGGAAPA-APPPAPAPAAPAA------PAGAAPAQPAPAPAATPPAGQADDPAAQ 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1560 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1639
Cdd:PRK07764  721 PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800


                  ..
gi 46852172  1640 PA 1641
Cdd:PRK07764  801 AE 802
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1413-1656 1.09e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1413 DVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVksfvPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIM 1492
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1493 VQSASPdIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKP-AKVPSPPPVIAVTAvTPAPEAQDGPPSPLSEASSGYFSH 1571
Cdd:PHA03247 2937 PRPQPP-LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrFRVPQPAPSREAPA-SSTPPLTGHSLSRVSSWASSLALH 3014

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1572 SVST---ATLSDALGP-----GLDAAAPPGSMPTAPEAE--------PEAPISHPPPPTAVPAEEPPGPQQLVSPgrerP 1635
Cdd:PHA03247 3015 EETDpppVSLKQTLWPpddteDSDADSLFDSDSERSDLEaldplppePHDPFAHEPDPATPEAGARESPSSQFGP----P 3090

                         250       260
                  ....*....|....*....|.
gi 46852172  1636 DLEAPAPGSPFRVRRVRASEL 1656
Cdd:PHA03247 3091 PLSANAALSRRYVRSTGRSAL 3111
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 1477-1703 1.29e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1477 GKRPSPLAhqPVPRI---MVqsaspdirVTRM-------EEAQPEMGPDVLVQTMGAPALKicDKPAKVPSPPPVIAVTA 1546
Cdd:PRK07994  335 GRKDLPLA--PDRRMgveMT--------LLRMlafhpaaPLPEPEVPPQSAAPAASAQATA--APTAAVAPPQAPAVPPP 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1547 VTPAPEAQdgPPSPLSEAssgyfshsvsTATLSDALgPGLDAAAPPgsmPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQ 1626
Cdd:PRK07994  403 PASAPQQA--PAVPLPET----------TSQLLAAR-QQLQRAQGA---TKAKKSEPAAASRARPVNSALERLASVRPAP 466

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172  1627 LVSPgrerpdlEAPAPGSPFRVRRVRASElrsfsrmLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLRE 1703
Cdd:PRK07994  467 SALE-------KAPAKKEAYRWKATNPVE-------VKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAL 529
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1539-1645 1.69e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 42.83  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1539 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1614
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273

                          90       100       110
                  ....*....|....*....|....*....|.
gi 46852172  1615 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1645
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
1435-1652 1.70e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 43.05  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1435 NNHSPDPGLSNLAASylNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGP 1514
Cdd:PRK12727   30 SNRRTAEGIEIVAAS--NYDEELVQRALETARSDTPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAED 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1515 DVLVQTMGAPALKICDKPAKVP-----SPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSD-ALGPGLDA 1588
Cdd:PRK12727  108 MIAAMALRQPVSVPRQAPAAAPvraasIPSPAAQALAHAAAVRTAPRQEHALSAVPEQLFADFLTTAPVPRaPVQAPVVA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1589 AAPPGSMPTAPEAEPEAPISH--------------PPPPTAVPAEEPP---GPQQLVSPGRERpdLEAPAPGSPFRVRRV 1651
Cdd:PRK12727  188 APAPVPAIAAALAAHAAYAQDddeqldddgfdlddALPQILPPAALPPivvAPAAPAALAAVA--AAAPAPQNDEELKQL 265


                  .
gi 46852172  1652 R 1652
Cdd:PRK12727  266 R 266
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
 1532-1699 1.86e-03

poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA.


Pssm-ID: 130706 [Multi-domain]  Cd Length: 612  Bit Score: 43.14  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1532 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1603
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172   1604 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1677
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447

                          170       180
                   ....*....|....*....|...
gi 46852172   1678 PA-PGAGGQALASDSEEADEVPE 1699
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 1545-1642 1.89e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.87  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1545 TAVTPAPEAQDGPPsplseassgyfshsvsTATLSDALGPGLDAAAPPGSMPTA--PEAEPEAPISHPPPPTAVPAEEPP 1622
Cdd:PRK14950  358 ALLVPVPAPQPAKP----------------TAAAPSPVRPTPAPSTRPKAAAAAniPPKEPVRETATPPPVPPRPVAPPV 421

                          90       100
                  ....*....|....*....|....*...
gi 46852172  1623 GPQQ--------LVSPGRERPDLEAPAP 1642
Cdd:PRK14950  422 PHTPesapkltrAAIPVDEKPKYTPPAP 449
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
 368-444 2.00e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 41.89  E-value: 2.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46852172  368 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 444
Cdd:COG5493   36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 1582-1699 2.22e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1582 LGPGLDAAAPPGSMPTAPEAEPEApiSHPPPPTAVPAEEPPGPqqlvsPGRERPdLEAPAPGSPFRVRRVRASELRSFSR 1661
Cdd:PRK07764  385 LGVAGGAGAPAAAAPSAAAAAPAA--APAPAAAAPAAAAAPAP-----AAAPQP-APAPAPAPAPPSPAGNAPAGGAPSP 456

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 46852172  1662 MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1699
Cdd:PRK07764  457 PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
368-432 2.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46852172   368 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 432
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1523-1688 3.55e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1523 APALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGldAAAPPGSMPTAPE 1600
Cdd:PHA03307  776 EPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADaaSRTASKRKSRSHTPDGGSESSGPARPPG--AAARPPPARSSES 853

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1601 AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPG-SPFRVRRVRASELRSFSRMLAGDP---GC---SPGA 1673
Cdd:PHA03307  854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPpAGAPAPRPRPAPRVKLGPMPPGGPdprGGfrrVPPG 933

                         170
                  ....*....|....*
gi 46852172  1674 EGNAPAPGAggQALA 1688
Cdd:PHA03307  934 DLHTPAPSA--AALA 946
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 1421-1642 7.32e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 40.99  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1421 RGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDE-------KRGKRPSPLAHQPVPRIMV 1493
Cdd:COG3266  109 LLRAAALLLLKLLLLLLTLLLLVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLlllalqdIQGTLQALGAVAALLGLRK 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172 1494 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSP---PPVIAVTAVTPAPEAQDGPPSPLSEASSGYFS 1570
Cdd:COG3266  189 AEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAagaAEVLTARLVLLLLIIGSALKAPSQASSASAPA 268

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46852172 1571 HSVSTATLSDALGPGldAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSP--GRERPDLEAPAP 1642
Cdd:COG3266  269 TTSLGEQQEVSLPPA--VAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKpvVTETAAPAAPAP 340
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
611-760 7.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  611 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 683
Cdd:COG4913  612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46852172  684 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 760
Cdd:COG4913  688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
flhF PRK06995
flagellar biosynthesis protein FlhF;
1586-1680 8.95e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 40.72  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46852172  1586 LDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAG 1665
Cdd:PRK06995   48 LAALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEP--APWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125

                          90
                  ....*....|....*
gi 46852172  1666 DPGCSPGAEGNAPAP 1680
Cdd:PRK06995  126 ENAARRLARAAAAAP 140
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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