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Conserved domains on  [gi|767950714|ref|XP_011542761|]
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kinesin-like protein KIF13B isoform X4 [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 ...
3-296 8.52e-175

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: 531.93  E-value: 8.52e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    3 ESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKV 82
Cdd:cd01365    64 DSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   83 EVSYMEIYNEKVRDLLDPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHA 160
Cdd:cd01365   144 EVSYMEIYNEKVRDLLNPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  161 VFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKF 238
Cdd:cd01365   224 VFTIVLTQKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSF 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  239 VPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 296
Cdd:cd01365   304 IPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
383-481 4.08e-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: 4.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  383 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 462
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 767950714  463 HHGDRILWGNNHFFRLNLP 481
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1661-1724 3.18e-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: 3.18e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950714  1661 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1724
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
Kinesin_assoc super family cl24686
Kinesin-associated;
293-405 7.00e-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: 7.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   293 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 327
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   328 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 390
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 767950714   391 ADPALNELLVYYLKE 405
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
692-738 1.83e-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: 1.83e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714   692 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 738
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1381-1640 1.50e-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: 69.97  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1449
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1450 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1526
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1527 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1598
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767950714 1599 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1640
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 ...
1157-1214 7.27e-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: 50.66  E-value: 7.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950714  1157 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1214
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
bMERB_dom super family cl48129
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1035-1079 1.38e-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: 1.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714  1035 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1079
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
547-696 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 767950714  547 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 619
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  620 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 696
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 ...
3-296 8.52e-175

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: 531.93  E-value: 8.52e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    3 ESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKV 82
Cdd:cd01365    64 DSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   83 EVSYMEIYNEKVRDLLDPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHA 160
Cdd:cd01365   144 EVSYMEIYNEKVRDLLNPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  161 VFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKF 238
Cdd:cd01365   224 VFTIVLTQKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSF 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  239 VPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 296
Cdd:cd01365   304 IPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-296 1.76e-141

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: 440.86  E-value: 1.76e-141
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714      9 YAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYME 88
Cdd:smart00129   57 TASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLE 135
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714     89 IYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:smart00129  136 IYNEKIRDLLNP--SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQ 213
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    169 TLYDVKSGTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTW 248
Cdd:smart00129  214 KIKNSSSGSG--KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTR 287
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 767950714    249 LLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 296
Cdd:smart00129  288 LLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
10-289 2.40e-139

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 2.40e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEI 89
Cdd:pfam00225   52 ATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEI 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    90 YNEKVRDLLDPKGSRQ-TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:pfam00225  131 YNEKIRDLLSPSNKNKrKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQ 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   169 TLYDVKSGTSGeKVGKLSLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLT 247
Cdd:pfam00225  211 RNRSTGGEESV-KTGKLNLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLT 284
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 767950714   248 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:pfam00225  285 RLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
10-375 2.64e-93

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 314.75  E-value: 2.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEI 89
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDL-SMTKDFAVSISYLEI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   90 YNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 169
Cdd:COG5059   147 YNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS- 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  170 lYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagKNKNKFVPYRDSVLTWL 249
Cdd:COG5059   224 -KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----KKKSGHIPYRESKLTRL 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  250 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPNARIIRDL---REEVEKLREQLTKA 321
Cdd:COG5059   297 LQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREIEEIKFDLsedRSEIEILVFREQSQ 376
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950714  322 EAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISLQSS 375
Cdd:COG5059   377 LSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTLQFL 435
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-315 1.51e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.12  E-value: 1.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    3 ESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQK 72
Cdd:PLN03188  137 DSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   73 EE----NEEQSFKVEVSYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAA 148
Cdd:PLN03188  217 EQikhaDRQLKYQCRCSFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGA 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  149 TNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAD 228
Cdd:PLN03188  295 TSINAESSRSHSVFTCVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  229 QSAgKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--AR 302
Cdd:PLN03188  375 ISQ-TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflRE 453
                         330
                  ....*....|...
gi 767950714  303 IIRDLREEVEKLR 315
Cdd:PLN03188  454 VIRQLRDELQRVK 466
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
383-481 4.08e-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: 4.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  383 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 462
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 767950714  463 HHGDRILWGNNHFFRLNLP 481
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1661-1724 3.18e-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: 3.18e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950714  1661 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1724
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
1661-1725 5.78e-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: 5.78e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714   1661 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1725
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
293-405 7.00e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.38  E-value: 7.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   293 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 327
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   328 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 390
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 767950714   391 ADPALNELLVYYLKE 405
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
692-738 1.83e-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: 1.83e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714   692 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 738
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
1661-1730 3.97e-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: 74.72  E-value: 3.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1661 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1730
Cdd:COG5244     7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
PHA03247 PHA03247
large tegument protein UL36; Provisional
1381-1640 1.50e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1449
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1450 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1526
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1527 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1598
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767950714 1599 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1640
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
407-470 3.61e-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: 3.61e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950714   407 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 470
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
1396-1710 6.42e-08

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.38  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1396 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1475
Cdd:COG5180   174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1476 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1550
Cdd:COG5180   253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1551 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1614
Cdd:COG5180   332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1615 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1692
Cdd:COG5180   412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484
                         330
                  ....*....|....*...
gi 767950714 1693 DLPSGKNDGSIGGKQYFR 1710
Cdd:COG5180   485 LGVRPDAILGGNVAPASG 502
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
1311-1612 8.22e-08

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: 56.71  E-value: 8.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1311 LSR-RSISSpnvNRVSVWNQALCCAWDFSPLLF----SWLSGSRqdliPSYSLGSNKGRWESQQDVSQTTVSRGIA---- 1381
Cdd:pfam13254   36 LSRqNSFAS---NRGSVAGPSGSLSPGLSPTKLsregSPESTSR----PSSSHSEATIVRHSKDDERPSTPDEGFVkpal 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1382 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-----PQMPKLLKSLFPVRDEKRGKRPSPLAHQP-----VPRIMVQ 1451
Cdd:pfam13254  109 PRHSRSSSALSNTGSEEDSPSLPTSPPSPSKTMDpkrwsPTKSSWLESALNRPESPKPKAQPSQPAQPawmkeLNKIRQS 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1452 SASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASS 1523
Cdd:pfam13254  189 RASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPP 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1524 GYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP- 1602
Cdd:pfam13254  262 PKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPp 338
                          330
                   ....*....|....*
gi 767950714  1603 --FRV---RRVRASE 1612
Cdd:pfam13254  339 kdFRAnlrSREVPKD 353
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1157-1214 7.27e-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: 50.66  E-value: 7.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950714  1157 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1214
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1490-1611 8.61e-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: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1490 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1561
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767950714 1562 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1611
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
404-478 1.11e-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: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714  404 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 478
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1035-1079 1.38e-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: 1.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714  1035 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1079
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1381-1602 2.18e-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: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1460
Cdd:NF033839  294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1461 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1539
Cdd:NF033839  356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714 1540 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1602
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 ...
1462-1598 4.88e-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: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1462 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1530
Cdd:cd21975    12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950714 1531 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1598
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 ...
1536-1620 8.84e-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: 43.84  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1536 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1612
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101

                  ....*...
gi 767950714 1613 LRSFSRML 1620
Cdd:NF041121  102 PLELARAL 109
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1496-1602 1.68e-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: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1496 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1571
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767950714 1572 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1602
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
1489-1656 1.82e-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: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1489 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1560
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1561 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1634
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
                          170       180
                   ....*....|....*....|...
gi 767950714  1635 PA-PGAGGQALASDSEEADEVPE 1656
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
304-380 1.93e-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: 1.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950714  304 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 380
Cdd:COG5493    36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
304-368 2.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714  304 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 368
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
547-696 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 767950714  547 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 619
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  620 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 696
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 ...
3-296 8.52e-175

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: 531.93  E-value: 8.52e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    3 ESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKV 82
Cdd:cd01365    64 DSEDPNYASQEQVYEDLGEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   83 EVSYMEIYNEKVRDLLDPK--GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHA 160
Cdd:cd01365   144 EVSYMEIYNEKVRDLLNPKpkKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHA 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  161 VFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKN--KNKF 238
Cdd:cd01365   224 VFTIVLTQKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkKSSF 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  239 VPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 296
Cdd:cd01365   304 IPYRDSVLTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
KISc smart00129
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ...
9-296 1.76e-141

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: 440.86  E-value: 1.76e-141
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714      9 YAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTqKEENEEQSFKVEVSYME 88
Cdd:smart00129   57 TASQEDVFEETAAPLVDSVLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKI-DKREEGWQFSVKVSYLE 135
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714     89 IYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:smart00129  136 IYNEKIRDLLNP--SSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQ 213
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    169 TLYDVKSGTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSagknKNKFVPYRDSVLTW 248
Cdd:smart00129  214 KIKNSSSGSG--KASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS----KSRHIPYRDSKLTR 287
                           250       260       270       280
                    ....*....|....*....|....*....|....*....|....*...
gi 767950714    249 LLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVN 296
Cdd:smart00129  288 LLQDSLGGNSKTLMIANVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
Kinesin pfam00225
Kinesin motor domain;
10-289 2.40e-139

Kinesin motor domain;


Pssm-ID: 459720 [Multi-domain]  Cd Length: 326  Bit Score: 434.69  E-value: 2.40e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYMEI 89
Cdd:pfam00225   52 ATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK-ERSEFSVKVSYLEI 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    90 YNEKVRDLLDPKGSRQ-TLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:pfam00225  131 YNEKIRDLLSPSNKNKrKLRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQ 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   169 TLYDVKSGTSGeKVGKLSLVDLAGSERATKTGAA-GDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLT 247
Cdd:pfam00225  211 RNRSTGGEESV-KTGKLNLVDLAGSERASKTGAAgGQRLKEAANINKSLSALGNVISALAD-----KKSKHIPYRDSKLT 284
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 767950714   248 WLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:pfam00225  285 RLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFASRAKNI 326
KISc cd00106
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ...
10-287 6.35e-129

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: 406.26  E-value: 6.35e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD-QPGLIPRLCSGLFERTQKEENEEQSFKVEVSYME 88
Cdd:cd00106    56 STQEEVYEGTAKPLVDSALEGYNGTIFAYGQTGSGKTYTMLGPDPeQRGIIPRALEDIFERIDKRKETKSSFSVSASYLE 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   89 IYNEKVRDLLDPKgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:cd00106   136 IYNEKIYDLLSPV-PKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  169 tlYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTW 248
Cdd:cd00106   215 --RNREKSGESVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-----GQNKHIPYRDSKLTR 287
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767950714  249 LLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 287
Cdd:cd00106   288 LLQDSLGGNSKTIMIACISPSSENFEETLSTLRFASRAK 326
KISc_C_terminal cd01366
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ...
10-291 5.09e-108

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: 347.66  E-value: 5.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLgENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEENEEQSFKVEVSYMEI 89
Cdd:cd01366    57 ASQEDVFEEV-SPLVQSALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGWSYTIKASMLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   90 YNEKVRDLLDPKGSRQT-LKVREHSVLGP-YVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLt 167
Cdd:cd01366   136 YNETIRDLLAPGNAPQKkLEIRHDSEKGDtTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI- 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  168 htlydvkSGT---SGEK-VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdqsagkNKNKFVPYRD 243
Cdd:cd01366   215 -------SGRnlqTGEIsVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR------QKQSHIPYRN 281
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767950714  244 SVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVN 291
Cdd:cd01366   282 SKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNSLRFASKVNSCEL 329
KISc_KIF3 cd01371
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ...
13-289 1.79e-106

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: 343.67  E-value: 1.79e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   13 DIVFKCLGENILQnafdGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEENEEQsFKVEVSYMEI 89
Cdd:cd01371    67 DETARPLVDSVLE----GYNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQ-FLVRVSYLEI 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   90 YNEKVRDLLDpKGSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHT 169
Cdd:cd01371   142 YNEEIRDLLG-KDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECS 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  170 lYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVLTWL 249
Cdd:cd01371   221 -EKGEDGENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD-----GKSTHIPYRDSKLTRL 294
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767950714  250 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:cd01371   295 LQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
KISc_KHC_KIF5 cd01369
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ...
10-289 2.36e-104

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: 336.99  E-value: 2.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP---GLIPRLCSGLFERTQKEeNEEQSFKVEVSY 86
Cdd:cd01369    55 TTQEDVYNFAAKPIVDDVLNGYNGTIFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSM-DENLEFHVKVSY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   87 MEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITL 166
Cdd:cd01369   134 FEIYMEKIRDLLDV--SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  167 THTlyDVKSGTSgeKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagkNKNKFVPYRDSVL 246
Cdd:cd01369   212 KQE--NVETEKK--KSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD-----GKKTHIPYRDSKL 282
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767950714  247 TWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:cd01369   283 TRILQDSLGGNSRTTLIICCSPSSYNESETLSTLRFGQRAKTI 325
KISc_CENP_E cd01374
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ...
15-289 3.12e-102

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: 330.83  E-value: 3.12e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   15 VFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQkeENEEQSFKVEVSYMEIYNEKV 94
Cdd:cd01374    56 VYELIAKPVVKSALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQ--DTPDREFLLRVSYLEIYNEKI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   95 RDLLDPKGsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHTLYDVK 174
Cdd:cd01374   134 NDLLSPTS--QNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGEL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  175 SGtSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqSAGKnKNKFVPYRDSVLTWLLKDSL 254
Cdd:cd01374   212 EE-GTVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGK-VGGHIPYRDSKLTRILQPSL 286
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767950714  255 GGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:cd01374   287 GGNSRTAIICTITPAESHVEETLNTLKFASRAKKI 321
KISc_KIF4 cd01372
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ...
11-289 4.39e-101

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: 328.52  E-value: 4.39e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   11 GQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA------DQPGLIPRLCSGLFERTQKEENEEQsFKVEV 84
Cdd:cd01372    53 EQEEVYNTCVAPLVDGLFEGYNATVLAYGQTGSGKTYTMGTAYtaeedeEQVGIIPRAIQHIFKKIEKKKDTFE-FQLKV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   85 SYMEIYNEKVRDLLDPKG-SRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFK 163
Cdd:cd01372   132 SFLEIYNEEIRDLLDPETdKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFT 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  164 ITLTHTLYDVKSGTSGEK------VGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAgknKNK 237
Cdd:cd01372   212 ITLEQTKKNGPIAPMSADdknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESK---KGA 288
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767950714  238 FVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:cd01372   289 HVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
KISc_KIP3_like cd01370
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ...
9-289 1.67e-100

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: 326.99  E-value: 1.67e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    9 YAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEnEEQSFKVEVSYME 88
Cdd:cd01370    72 TSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLK-DEKEFEVSMSYLE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   89 IYNEKVRDLLDPKGSRqtLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTH 168
Cdd:cd01370   151 IYNETIRDLLNPSSGP--LELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQ 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  169 TlYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsaGKNKNKFVPYRDSVLTW 248
Cdd:cd01370   229 Q-DKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD---PGKKNKHIPYRDSKLTR 304
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 767950714  249 LLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHI 289
Cdd:cd01370   305 LLKDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
KISc_KLP2_like cd01373
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ...
12-298 1.91e-94

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: 309.82  E-value: 1.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   12 QDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQP--------GLIPRLCSGLFERTQKEEN---EEQSF 80
Cdd:cd01373    55 QESVFQSVGKPIVESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEkagEGKSF 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   81 KVEVSYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHA 160
Cdd:cd01373   135 LCKCSFLEIYNEQIYDLLDP--ASRNLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHA 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  161 VFKITLTHtlYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQSAGKNKNkfVP 240
Cdd:cd01373   213 VFTCTIES--WEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRH--VC 288
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  241 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 298
Cdd:cd01373   289 YRDSKLTFLLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
10-375 2.64e-93

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 314.75  E-value: 2.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEeNEEQSFKVEVSYMEI 89
Cdd:COG5059    68 ATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDL-SMTKDFAVSISYLEI 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   90 YNEKVRDLLDPKgsRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLTHt 169
Cdd:COG5059   147 YNEKIYDLLSPN--EESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELAS- 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  170 lYDVKSGTSGEkvGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsagKNKNKFVPYRDSVLTWL 249
Cdd:COG5059   224 -KNKVSGTSET--SKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD----KKKSGHIPYRESKLTRL 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  250 LKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE-----DPNARIIRDL---REEVEKLREQLTKA 321
Cdd:COG5059   297 LQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSssdssREIEEIKFDLsedRSEIEILVFREQSQ 376
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950714  322 EAMKSPELKDR--LEESEKLIQEMTVT---WEEKLRKTEEIAQERQKQLESLGISLQSS 375
Cdd:COG5059   377 LSQSSLSGIFAymQSLKKETETLKSRIdliMKSIISGTFERKKLLKEEGWKYKSTLQFL 435
KISc_BimC_Eg5 cd01364
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ...
10-298 6.58e-88

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: 291.15  E-value: 6.58e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMG-----------TADQPGLIPRLCSGLFERTqkeENEEQ 78
Cdd:cd01364    61 AKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKL---EDNGT 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   79 SFKVEVSYMEIYNEKVRDLLDPKGS-RQTLKVREHS--VLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEES 155
Cdd:cd01364   138 EYSVKVSYLEIYNEELFDLLSPSSDvSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQS 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  156 SRSHAVFKITLthtlYDVKSGTSGE---KVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADqsag 232
Cdd:cd01364   218 SRSHSVFSITI----HIKETTIDGEelvKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---- 289
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950714  233 knKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNED 298
Cdd:cd01364   290 --RAPHVPYRESKLTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
KISc_KIF23_like cd01368
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ...
10-287 3.74e-75

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: 254.24  E-value: 3.74e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFertqkeeNEEQSFKVEVSYMEI 89
Cdd:cd01368    67 TTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIF-------NSIGGYSVFVSYIEI 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   90 YNEKVRDLLDPKGS-----RQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKI 164
Cdd:cd01368   140 YNEYIYDLLEPSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTI 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  165 TL----THTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAdQSAGKNKNKFVP 240
Cdd:cd01368   220 KLvqapGDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLR-ENQLQGTNKMVP 298
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767950714  241 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 287
Cdd:cd01368   299 FRDSKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
PLN03188 PLN03188
kinesin-12 family protein; Provisional
3-315 1.51e-74

kinesin-12 family protein; Provisional


Pssm-ID: 215621 [Multi-domain]  Cd Length: 1320  Bit Score: 274.12  E-value: 1.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    3 ESVKEKYAGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTA----------DQPGLIPRLCSGLFERTQK 72
Cdd:PLN03188  137 DSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   73 EE----NEEQSFKVEVSYMEIYNEKVRDLLDPkgSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAA 148
Cdd:PLN03188  217 EQikhaDRQLKYQCRCSFLEIYNEQITDLLDP--SQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGA 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  149 TNMNEESSRSHAVFKITLTHTLYDVKSGTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALAD 228
Cdd:PLN03188  295 TSINAESSRSHSVFTCVVESRCKSVADGLSSFKTSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAE 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  229 QSAgKNKNKFVPYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAKHIVNHAVVNE----DPN--AR 302
Cdd:PLN03188  375 ISQ-TGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEvmqdDVNflRE 453
                         330
                  ....*....|...
gi 767950714  303 IIRDLREEVEKLR 315
Cdd:PLN03188  454 VIRQLRDELQRVK 466
KISc_KIF9_like cd01375
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ...
10-287 8.56e-74

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: 249.80  E-value: 8.56e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   10 AGQDIVFKCLGENILQNAFDGYNACIFAYGQTGSGKSYTMMGTAD---QPGLIPRLCSGLFErtQKEENEEQSFKVEVSY 86
Cdd:cd01375    59 ASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFR--MIEERPTKAYTVHVSY 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   87 MEIYNEKVRDLLDPK----GSRQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVF 162
Cdd:cd01375   137 LEIYNEQLYDLLSTLpyvgPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIF 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  163 KITL---THTLYDVKSGTSgekvgKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALADQsagknKNKFV 239
Cdd:cd01375   217 TIHLeahSRTLSSEKYITS-----KLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-----DRTHV 286
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767950714  240 PYRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 287
Cdd:cd01375   287 PFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
FHA_KIF13B cd22730
forkhead associated (FHA) domain found in kinesin-like protein KIF13B; KIF13B, also called ...
383-481 4.08e-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: 4.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  383 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 462
Cdd:cd22730     1 KCFLVNLNADPALNELLVYYLKEHTLIGSADSQDIQLCGMGILPEHCIIDITPEGQVMLTPQKNTRTFVNGSAVTSPIQL 80
                          90
                  ....*....|....*....
gi 767950714  463 HHGDRILWGNNHFFRLNLP 481
Cdd:cd22730    81 HHGDRILWGNNHFFRINLP 99
KISc_KIF2_like cd01367
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ...
23-287 1.71e-66

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: 228.72  E-value: 1.71e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   23 ILQNAFDGYNACIFAYGQTGSGKSYTMMG----TADQPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYNEKVRDLL 98
Cdd:cd01367    75 LVPHIFEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDN-LGVTVSFFEIYGGKVFDLL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   99 DPKgsrQTLKVREHSVLGPYVDGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHAVFKITLthtlydvKSGTS 178
Cdd:cd01367   154 NRK---KRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  179 GEKVGKLSLVDLAGSERATKTGAAG-DRLKEGSNINKSLTTLGLVISALADQSAgknknkFVPYRDSVLTWLLKDSL-GG 256
Cdd:cd01367   224 NKLHGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA------HIPFRGSKLTQVLKDSFiGE 297
                         250       260       270
                  ....*....|....*....|....*....|.
gi 767950714  257 NSKTAMVATVSPAADNYDETLSTLRYADRAK 287
Cdd:cd01367   298 NSKTCMIATISPGASSCEHTLNTLRYADRVK 328
KISc_KID_like cd01376
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ...
4-287 7.08e-63

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: 217.76  E-value: 7.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    4 SVKEKYAGQdivFKClgenILQNAFDGYNACIFAYGQTGSGKSYTMMGTADQPGLIPRLCSGLFERTQKEEneeQSFKVE 83
Cdd:cd01376    57 TQEDIYARE---VQP----IVPHLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLLQMTRKEA---WALSFT 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   84 VSYMEIYNEKVRDLLDPKGSRqtLKVRE---HSVLGPyvdGLSKLAVTSYKDIESLMSEGNKSRTVAATNMNEESSRSHA 160
Cdd:cd01376   127 MSYLEIYQEKILDLLEPASKE--LVIREdkdGNILIP---GLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  161 VFKITLTHTLYDVksgTSGEKVGKLSLVDLAGSERATKTGAAGDRLKEGSNINKSLTTLGLVISALadqsagKNKNKFVP 240
Cdd:cd01376   202 VLLIKVDQRERLA---PFRQRTGKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL------NKNLPRIP 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 767950714  241 YRDSVLTWLLKDSLGGNSKTAMVATVSPAADNYDETLSTLRYADRAK 287
Cdd:cd01376   273 YRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFAARSR 319
FHA_KIF13 cd22706
forkhead associated (FHA) domain found in the kinesin-like protein KIF13 family; The KIF13 ...
383-481 2.37e-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: 2.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  383 KCFLVNLNADPALNELLVYYLKEHTLIGSANS---QDIQLCGMGILPEHCIIDItSEGQVMLTPQKNTRTFVNGSSVSSP 459
Cdd:cd22706     1 KYYLVNLNADPSLNELLVYYLKEHTLIGRSDAptqQDIQLSGLGIQPEHCIITI-ENEDVYLTPLEGARTCVNGSIVTEK 79
                          90       100
                  ....*....|....*....|..
gi 767950714  460 IQLHHGDRILWGNNHFFRLNLP 481
Cdd:cd22706    80 TQLRHGDRILWGNNHFFRLNCP 101
FHA_KIF13A cd22729
forkhead associated (FHA) domain found in kinesin-like protein KIF13A; KIF13A, also called ...
383-486 1.39e-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: 1.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  383 KCFLVNLNADPALNELLVYYLKEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNTRTFVNGSSVSSPIQL 462
Cdd:cd22729     1 KCYLVNLNADPALNELLVYYLKDHTRVGADTSQDIQLFGIGIQPEHCVIDIAADGDVTLTPKENARTCVNGTLVCSVTQL 80
                          90       100
                  ....*....|....*....|....
gi 767950714  463 HHGDRILWGNNHFFRLNLPKKKKK 486
Cdd:cd22729    81 WHGDRILWGNNHFFRINLPKRKRR 104
FHA_KIF1 cd22705
forkhead associated (FHA) domain found in the kinesin-like protein KIF1 family; The KIF1 ...
386-479 7.71e-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: 7.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 461
Cdd:cd22705     4 LVNLNEDPLMSECLLYYIKPgITRVGRADAdvpQDIQLSGTHILEEHCTFE-NEDGVVTLEPCEGALTYVNGKRVTEPTR 82
                          90
                  ....*....|....*...
gi 767950714  462 LHHGDRILWGNNHFFRLN 479
Cdd:cd22705    83 LKTGSRVILGKNHVFRFN 100
FHA_KIF14 cd22707
forkhead associated (FHA) domain found in kinesin-like protein KIF14 and similar proteins; ...
386-481 3.85e-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: 3.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKE-HTLIGS--ANSQ-DIQLCGMGILPEHCIIdITSEGQVMLTPQKNTRTFVNGSSVSSPIQ 461
Cdd:cd22707    10 LVNLNEDPQLSEMLLYMLKEgQTRVGRskASSShDIQLSGALIADDHCTI-ENNGGKVTIIPVGDAETYVNGELISEPTV 88
                          90       100
                  ....*....|....*....|
gi 767950714  462 LHHGDRILWGNNHFFRLNLP 481
Cdd:cd22707    89 LHHGDRVILGGDHYFRFNHP 108
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
1661-1724 3.18e-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: 3.18e-30
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950714  1661 GEFVTVGAHKTGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRV 1724
Cdd:pfam01302    2 GDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
384-481 1.53e-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: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  384 CFLVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIdITSEGQVMLTPQKNT-RTFVNGSSVSS 458
Cdd:cd22709     1 PHLLNLNEDPQLSGVIVHFLQEgETTIGRADAepePDIVLSGLSIQKQHAVI-TNTDGKVTIEPVSPGaKVIVNGVPVTG 79
                          90       100
                  ....*....|....*....|...
gi 767950714  459 PIQLHHGDRILWGNNHFFRLNLP 481
Cdd:cd22709    80 ETELHHLDRVILGSNHLYVFVGP 102
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
4-225 1.36e-27

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: 110.90  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    4 SVKEKYAGQDIVFKcLGENILQNAFDGYN-ACIFAYGQTGSGKSYTMMGtadqpgLIPRLCSGLFERTQKEENEEQsfkv 82
Cdd:cd01363    24 RGFRRSESQPHVFA-IADPAYQSMLDGYNnQSIFAYGESGAGKTETMKG------VIPYLASVAFNGINKGETEGW---- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   83 evsymeiynekvrdlldpkgsrqtlkvrehsvlgpyvDGLSKLAVTSYKDIESLMSEGNKSRTvAATNMNEESSRSHAVF 162
Cdd:cd01363    93 -------------------------------------VYLTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFI 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950714  163 KItlthtlydvksgtsgekvgklsLVDLAGSERatktgaagdrlkegsnINKSLTTLGLVISA 225
Cdd:cd01363   135 EI----------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
1661-1725 5.78e-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: 5.78e-26
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714   1661 GEFVTVGAH-KTGVVRYVGPADFQEGTWVGVELDLP-SGKNDGSIGGKQYFRCNPGYGLLVRPSRVR 1725
Cdd:smart01052    2 GDRVEVGGGgRRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
Kinesin_assoc pfam16183
Kinesin-associated;
293-405 7.00e-25

Kinesin-associated;


Pssm-ID: 465047 [Multi-domain]  Cd Length: 177  Bit Score: 103.38  E-value: 7.00e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   293 AVVNEDPNARIIRDLREEVEKLREQL------------------------------TKAEAMKSP--------------- 327
Cdd:pfam16183    1 AVINEDPNNKLIRELKDEVARLRDLLyaqglgdiidtiahptkkrantpaanasaaTAAMAGASPspslsalssraasvs 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   328 -------------ELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG----DDKCFLVNLN 390
Cdd:pfam16183   81 slherimftpgseEAIERLKETEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGvfspKKTPHLVNLN 160
                          170
                   ....*....|....*
gi 767950714   391 ADPALNELLVYYLKE 405
Cdd:pfam16183  161 EDPLMSECLLYYIKD 175
FHA_KIF1B cd22727
forkhead associated (FHA) domain found in kinesin-like protein KIF1B; KIF1B, also called Klp, ...
386-483 1.60e-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: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVS 457
Cdd:cd22727     5 LVNLNEDPLMSECLLYYIKDGiTRVGQADAerrQDIVLSGAHIKEEHCIFrsERNNNGEVIVTlePCERSETYVNGKRVV 84
                          90       100
                  ....*....|....*....|....*.
gi 767950714  458 SPIQLHHGDRILWGNNHFFRLNLPKK 483
Cdd:cd22727    85 QPVQLRSGNRIIMGKNHVFRFNHPEQ 110
FHA_KIF1A cd22726
forkhead associated (FHA) domain found in kinesin-like protein KIF1A; KIF1A, also called ...
386-490 3.88e-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: 87.68  E-value: 3.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKEH-TLIGSANS---QDIQLCGMGILPEHCII--DITSEGQ--VMLTPQKNTRTFVNGSSVS 457
Cdd:cd22726     4 LVNLNEDPLMSECLLYYIKDGiTRVGREDAerrQDIVLSGHFIKEEHCIFrsDTRSGGEavVTLEPCEGADTYVNGKKVT 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767950714  458 SPIQLHHGDRILWGNNHFFRLNLPKKKKKaERE 490
Cdd:cd22726    84 EPSILRSGNRIIMGKSHVFRFNHPEQARQ-ERE 115
FHA_KIF1C cd22728
forkhead associated (FHA) domain found in kinesin-like protein KIF1C; KIF1C is a new ...
386-479 1.63e-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: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKEH-TLIGSANSqDIQLCGMGILPEHCII--DITSEGQVMLT--PQKNTRTFVNGSSVSSPI 460
Cdd:cd22728     4 LVNLNEDPLMSECLLYHIKDGvTRVGQVDV-DIKLSGQFIREQHCLFrsIPNPSGEVVVTlePCEGAETYVNGKQVTEPL 82
                          90
                  ....*....|....*....
gi 767950714  461 QLHHGDRILWGNNHFFRLN 479
Cdd:cd22728    83 VLKSGNRIVMGKNHVFRFN 101
FHA_KIF16 cd22708
forkhead associated (FHA) domain found in the kinesin-like protein KIF16 family; The KIF16 ...
386-481 3.77e-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: 3.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKE-HTLIGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 461
Cdd:cd22708    11 LIGIDDDLLSTGVVLYHLKEgKTRIGREDApqeQDIVLDGEDIEAEHCIIE-NVGGVVTLHPLPGALCAVNGQVITQPTR 89
                          90       100
                  ....*....|....*....|
gi 767950714  462 LHHGDRILWGNNHFFRLNLP 481
Cdd:cd22708    90 LTQGDVILLGKTNMFRFNHP 109
Microtub_bd pfam16796
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ...
12-98 5.46e-16

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


Pssm-ID: 465274 [Multi-domain]  Cd Length: 144  Bit Score: 76.49  E-value: 5.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714    12 QDIVFKCLgENILQNAFDGYNACIFAYGQTGSGKSytmmgtadqPGLIPRLCSGLFERTQKEENEEQsFKVEVSYMEIYN 91
Cdd:pfam16796   69 QEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGSGSN---------DGMIPRAREQIFRFISSLKKGWK-YTIELQFVEIYN 137

                   ....*..
gi 767950714    92 EKVRDLL 98
Cdd:pfam16796  138 ESSQDLL 144
FHA_AFDN cd22711
forkhead associated (FHA) domain found in afadin and similar proteins; Afadin, also called ...
384-481 2.74e-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: 2.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  384 CFLVNLNADPALNellvYYLKEH------TLIGSANS-----QDIQLCGMGILPEHCIIDITsEGQVMLTP-QKNTRTFV 451
Cdd:cd22711     2 PYLLELSPDGSDR----DKPRRHrlqpnvTEVGSERSpansgQFIQLFGPDILPRHCVITHM-EGVVTVTPaSQDAETYV 76
                          90       100       110
                  ....*....|....*....|....*....|
gi 767950714  452 NGSSVSSPIQLHHGDRILWGNNHFFRLNLP 481
Cdd:cd22711    77 NGQRIYETTMLQHGMVVQFGRSHTFRFCDP 106
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
404-475 1.16e-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: 1.16e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950714  404 KEHTLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTP-QKNTRTFVNGSSVSSPIQLHHGDRILWGNNHF 475
Cdd:cd22673    20 KKSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENlSTTNPTLVNGKAIEKSAELKDGDVITIGGRSF 92
KIF1B pfam12423
Kinesin protein 1B; This domain family is found in eukaryotes, and is approximately 50 amino ...
692-738 1.83e-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: 1.83e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714   692 LDNRLLDMRDLYQEWKECEEDNPVIRSYfkraDPFYDEQENHSLIGV 738
Cdd:pfam12423    1 LENRLVDMREMYQEYKEGEYSQHFEVDR----DPFYEPPENHNLIGV 43
FHA_PHLB1 cd22713
forkhead associated (FHA) domain found in pleckstrin homology-like domain family B member 1 ...
374-485 2.31e-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: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  374 SSGIKVGDDKCFLVNLNADPALNELLVYYLKE-HTLIGSANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNtRTFVN 452
Cdd:cd22713     7 GKALKVQTEKPHLVSLGSGRLSTAVTLLPLPEgKTTIGTAASDIISLQGPGVEPEHCYIE-NINGTVTLYPCGN-LCSVD 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767950714  453 GSSVSSPIQLHHGDRILWGNNHFFRLNLPKKKK 485
Cdd:cd22713    85 GLPITEPTRLTQGCMICLGRSNYFRFNHPAEAK 117
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
1661-1730 3.97e-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: 74.72  E-value: 3.97e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1661 GEFVTVGAHKtGVVRYVGPADFQEGTWVGVELDLPSGKNDGSIGGKQYFRCNPGYGLLVRPSRVRRATGP 1730
Cdd:COG5244     7 NDRVLLGDKF-GTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRPDDDSLLNGN 75
FHA_KIF16B cd22732
forkhead associated (FHA) domain found in kinesin-like protein KIF16B; KIF16B, also called ...
386-486 1.68e-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: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKE-HTLIG---SANSQDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 461
Cdd:cd22732    11 LIGIDDDLLSTGIILYHLKEgRTYVGrddATTEQDIVLHGLDLESEHCIFE-NLNGTVTLIPLNGAQCSVNGVQITEATQ 89
                          90       100
                  ....*....|....*....|....*
gi 767950714  462 LHHGDRILWGNNHFFRLNLPKKKKK 486
Cdd:cd22732    90 LNQGAVILLGRTNMFRFNHPKEAAK 114
PHA03247 PHA03247
large tegument protein UL36; Provisional
1381-1640 1.50e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 69.97  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNNhSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPL-----------AHQPVPRIM 1449
Cdd:PHA03247 2711 APHALVSATPLPP-GPAAARQASPALPAAPAPPAVPAGPAT-----PGGPARPARPPTTAgppapappaapAAGPPRRLT 2784
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1450 VQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKvPSPPPviavTAVTPAPEAQDGPPSPLSEASSGYF--- 1526
Cdd:PHA03247 2785 RPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAG-PLPPP----TSAQPTAPPPPPGPPPPSLPLGGSVapg 2859
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1527 --------SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPtavPAEEPPGPQqlvsPGRERPDLEAPA 1598
Cdd:PHA03247 2860 gdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQP---QAPPPPQPQ----PQPPPPPQPQPP 2932
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 767950714 1599 PGSPFRVRRVRASElrsfsrmlaGDPGCSPGAEGNAPAPGAG 1640
Cdd:PHA03247 2933 PPPPPRPQPPLAPT---------TDPAGAGEPSGAVPQPWLG 2965
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
407-470 3.61e-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: 3.61e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950714   407 TLIGSANSQDIQLCGMGILPEHCIIDITSEGQVMLTPQKNT-RTFVNGSSVSS-PIQLHHGDRILW 470
Cdd:pfam00498    1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGGRFYLEDLGSTnGTFVNGQRLGPePVRLKDGDVIRL 66
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
385-475 5.06e-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: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  385 FLVNLNADPALNELLVYylKEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNT-RTFVNGSSVSSPIQLH 463
Cdd:cd00060     1 RLIVLDGDGGGREFPLT--KGVVTIGRSPDCDIVLDDPSVSRRHARIEVD-GGGVYLEDLGSTnGTFVNGKRITPPVPLQ 77
                          90
                  ....*....|..
gi 767950714  464 HGDRILWGNNHF 475
Cdd:cd00060    78 DGDVIRLGDTTF 89
PHA03247 PHA03247
large tegument protein UL36; Provisional
1378-1656 6.64e-11

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 68.04  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1378 RGIAPAPAL-SVSPQNNHSPDP---GLSNLAASYLNPVKSFVPQMPKLLKSLFP--VRDEKRGKRPS--PLAHQPVPRIM 1449
Cdd:PHA03247 2605 RGDPRGPAPpSPLPPDTHAPDPpppSPSPAANEPDPHPPPTVPPPERPRDDPAPgrVSRPRRARRLGraAQASSPPQRPR 2684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1450 VQSASPDI-RVTRM-----EEAQPEMGPDVLVQTMGAP-----ALKICDKPAKVPSPPPVIAVTAV------TPAPEAQD 1512
Cdd:PHA03247 2685 RRAARPTVgSLTSLadpppPPPTPEPAPHALVSATPLPpgpaaARQASPALPAAPAPPAVPAGPATpggparPARPPTTA 2764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1513 GPPSPLSEAS-----------SGYFSHSVSTATLSDALGP--------GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAV 1573
Cdd:PHA03247 2765 GPPAPAPPAApaagpprrltrPAVASLSESRESLPSPWDPadppaavlAPAAALPPAASPAGPLPPPTSAQPTAPPPPPG 2844
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1574 PAEEPPGPQQLVSPG---RERPDLEAPA--PGSPFR--VRRVRASELRSFSRMLAGDPgcsPGAEgNAPAPGAGGQALAS 1646
Cdd:PHA03247 2845 PPPPSLPLGGSVAPGgdvRRRPPSRSPAakPAAPARppVRRLARPAVSRSTESFALPP---DQPE-RPPQPQAPPPPQPQ 2920
                         330
                  ....*....|
gi 767950714 1647 DSEEADEVPE 1656
Cdd:PHA03247 2921 PQPPPPPQPQ 2930
FHA_KIF16A_STARD9 cd22731
forkhead associated (FHA) domain found in StAR-related lipid transfer protein 9 (StARD9); ...
386-481 2.92e-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: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  386 LVNLNADPALNELLVYYLKEHTL-IGSANS---QDIQLCGMGILPEHCIIDiTSEGQVMLTPQKNTRTFVNGSSVSSPIQ 461
Cdd:cd22731    11 LIAMDDDILSTGVVLYHLREGTTkIGRSDSeqeQDIVLQGPWIERDHCMIH-NECGVVTLRPAQGAQCTVNGREVTESCR 89
                          90       100
                  ....*....|....*....|
gi 767950714  462 LHHGDRILWGNNHFFRLNLP 481
Cdd:cd22731    90 LSQGAVIVLGKTHKFRFNHP 109
FHA_RADIL-like cd22712
forkhead associated (FHA) domain found in the Ras-associating and dilute domain-containing ...
382-476 9.67e-10

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: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  382 DKCFLVNLNADPALNELLVYYLKEHT-LIGS----ANSQDIQLCGMGILPEHCII--------------DITSEGQVMLT 442
Cdd:cd22712     2 DYPYLLTLRGFSPKQDLLVYPLLEQViLVGSrtegARKVDISLRAPDILPQHCWIrrkpeplsddedsdKESADYRVVLS 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 767950714  443 PQKNTRTFVNGSSVSSPIQLHHGDRILWGNNHFF 476
Cdd:cd22712    82 PLRGAHVTVNGVPVLSETELHPGDLLGIGEHYLF 115
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1493-1651 2.29e-09

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 62.88  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1493 PSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA 1572
Cdd:PHA03307  114 PDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1573 V----PAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRmlagDPGCSPGAEGNAPAPGAGGQALASDS 1648
Cdd:PHA03307  194 PpstpPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE----SSGCGWGPENECPLPRPAPITLPTRI 269

                  ...
gi 767950714 1649 EEA 1651
Cdd:PHA03307  270 WEA 272
PHA03247 PHA03247
large tegument protein UL36; Provisional
1495-1638 3.45e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 62.26  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1495 PPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFShsvSTATLSDA-------LGPGLDAAAPPGSMPTAPeAEPEAPISHP 1567
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDRSVPPPRPAPRPSEPAVT---SRARRPDAppqsarpRAPVDDRGDPRGPAPPSP-LPPDTHAPDP 2626
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1568 PPPTAVP-AEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRA--------SELRSFSRMLAGDPGCSPGAEGNAPAPG 1638
Cdd:PHA03247 2627 PPPSPSPaANEPDPHPPPTVPPPERPR-DDPAPGRVSRPRRARRlgraaqasSPPQRPRRRAARPTVGSLTSLADPPPPP 2705
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1465-1639 1.40e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 59.89  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1465 AQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIA-VTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGL 1543
Cdd:PRK12323  375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPaAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1544 DAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDlEAPAPGSPFRVRRVRASELRSFSRMLAGD 1623
Cdd:PRK12323  455 AAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPP-EFASPAPAQPDAAPAGWVAESIPDPATAD 533
                         170
                  ....*....|....*.
gi 767950714 1624 PgcSPGAEGNAPAPGA 1639
Cdd:PRK12323  534 P--DDAFETLAPAPAA 547
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1489-1612 1.81e-08

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 59.34  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1489 PAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGyfshsvstatlsdalgpglDAAAPPGSMPTAPEAEPEAPISHPP 1568
Cdd:PRK14951  389 PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA-------------------PVAAPAAAAPAAAPAAAPAAVALAP 449
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767950714 1569 PPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASE 1612
Cdd:PRK14951  450 APPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1437-1607 1.95e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 59.61  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1437 PSPLAHQPVPrimvQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1516
Cdd:PRK07764  636 PAEASAAPAP----GVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPA---APPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1517 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1596
Cdd:PRK07764  709 PPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAED 788
                         170
                  ....*....|.
gi 767950714 1597 PAPGSPFRVRR 1607
Cdd:PRK07764  789 DAPSMDDEDRR 799
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1437-1756 2.54e-08

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 59.41  E-value: 2.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1437 PSPLAHQPV---PRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDG 1513
Cdd:PHA03307   28 PGDAADDLLsgsQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1514 PPSPLSEASSGYFSHSVS------TATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTA------VPAEEPPGP 1581
Cdd:PHA03307  108 PPGPSSPDPPPPTPPPASpppspaPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAalplssPEETARAPS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1582 qqlvSPGRERPDLEAPAPGSPfrvrrvRASELRSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREG 1661
Cdd:PHA03307  188 ----SPPAEPPPSTPPAAASP------RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1662 EFVTVGAHKTGVVRYVGpadfqegtWVGVELDLPSGKNDGSIGGK--QYFRCNPGYGLLVRPSRVRRATGPVRRRSTGLR 1739
Cdd:PHA03307  258 PRPAPITLPTRIWEASG--------WNGPSSRPGPASSSSSPRERspSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
                         330
                  ....*....|....*..
gi 767950714 1740 LGAPEARRSATLSGSAT 1756
Cdd:PHA03307  330 SSSSESSRGAAVSPGPS 346
KIP1 COG5059
Kinesin-like protein [Cytoskeleton];
15-226 4.73e-08

Kinesin-like protein [Cytoskeleton];


Pssm-ID: 227392 [Multi-domain]  Cd Length: 568  Bit Score: 57.83  E-value: 4.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   15 VFKCLGENIlQNAFDGynacIFAYGQTGSGKSYTMMgtaDQPGLIPRLC-SGLFERTQKEENEEQSFKVEVSYMEIY-NE 92
Cdd:COG5059   370 VFREQSQLS-QSSLSG----IFAYMQSLKKETETLK---SRIDLIMKSIiSGTFERKKLLKEEGWKYKSTLQFLRIEiDR 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714   93 KVRDLLDPKGSRQTLKVREHSVLGPYVDGLSKLA-VTSYKDIESLMSegnKSRTVAATNMNEESSRSHAVFKitlthtly 171
Cdd:COG5059   442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPeETSDRVESEKAS---KLRSSASTKLNLRSSRSHSKFR-------- 510
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767950714  172 DVKSG-TSGEKVGKLSLVDLAGSERaTKTGAAGDRLKEGSNINKSLTTLGLVISAL 226
Cdd:COG5059   511 DHLNGsNSSTKELSLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHAL 565
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1480-1656 4.93e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 58.07  E-value: 4.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1480 APALKICDKPAKVPSPPPViAVTAVTPAPEAQDGPPSPLSEASSGYFSHS--------VSTATLSDALGPGLDAAAPPGS 1551
Cdd:PRK07764  602 APASSGPPEEAARPAAPAA-PAAPAAPAPAGAAAAPAEASAAPAPGVAAPehhpkhvaVPDASDGGDGWPAKAGGAAPAA 680
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1552 MPTAPEAEPEAPISHPPPPTAVPAE--EPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPG 1629
Cdd:PRK07764  681 PPPAPAPAAPAAPAGAAPAQPAPAPaaTPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
                         170       180
                  ....*....|....*....|....*..
gi 767950714 1630 AEGNAPAPGAGGQALASDSEEADEVPE 1656
Cdd:PRK07764  761 PPAPAPAAAPAAAPPPSPPSEEEEMAE 787
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
1396-1710 6.42e-08

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 57.38  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1396 PDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSaSPDIRVTRMEEAQPEMGPDVLV 1475
Cdd:COG5180   174 LPPPAEKLDKVLTEPRDALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPRPEAAS-SPKVDPPSTSEARSRPATVDAQ 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1476 QTMGAPALKICDKPAKV----PSPPPVIAVTAVTPAPEAqDGPPSPLSEASSGYFSHSVSTATLSDALGPG-LDAAAPPG 1550
Cdd:COG5180   253 PEMRPPADAKERRRAAIgdtpAAEPPGLPVLEAGSEPQS-DAPEAETARPIDVKGVASAPPATRPVRPPGGaRDPGTPRP 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1551 SMPT-APEAEPEAPISHPPPPTAVPAEEP-----PGPQQLVSPGRE-------RPDLEAPAPGSPFR---VRRVRASELR 1614
Cdd:COG5180   332 GQPTeRPAGVPEAASDAGQPPSAYPPAEEavpgkPLEQGAPRPGSSggdgapfQPPNGAPQPGLGRRgapGPPMGAGDLV 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1615 SFSRMLAGDPGCSPGAEGNAP--APGAGGQALASDSEEADEVPEwlregefVTVGAHKTGVVRYVGPADFQEGTWVGVEL 1692
Cdd:COG5180   412 QAALDGGGRETASLGGAAGGAgqGPKADFVPGDAESVSGPAGLA-------DQAGAAASTAMADFVAPVTDATPVDVADV 484
                         330
                  ....*....|....*...
gi 767950714 1693 DLPSGKNDGSIGGKQYFR 1710
Cdd:COG5180   485 LGVRPDAILGGNVAPASG 502
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
1311-1612 8.22e-08

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: 56.71  E-value: 8.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1311 LSR-RSISSpnvNRVSVWNQALCCAWDFSPLLF----SWLSGSRqdliPSYSLGSNKGRWESQQDVSQTTVSRGIA---- 1381
Cdd:pfam13254   36 LSRqNSFAS---NRGSVAGPSGSLSPGLSPTKLsregSPESTSR----PSSSHSEATIVRHSKDDERPSTPDEGFVkpal 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1382 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-----PQMPKLLKSLFPVRDEKRGKRPSPLAHQP-----VPRIMVQ 1451
Cdd:pfam13254  109 PRHSRSSSALSNTGSEEDSPSLPTSPPSPSKTMDpkrwsPTKSSWLESALNRPESPKPKAQPSQPAQPawmkeLNKIRQS 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1452 SASPDI-RVTRMEEAQPemgpdvlVQTMGAPALKICDKPAKVPSPPPVI-------AVTAVTPAPEAQDGPPSPLSEASS 1523
Cdd:pfam13254  189 RASVDLgRPNSFKEVTP-------VGLMRSPAPGGHSKSPSVSGISADSsptkeepSEEADTLSTDKEQSPAPTSASEPP 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1524 GYFSHSVSTATLSDAlgPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRErPDLEAPAPGSP- 1602
Cdd:pfam13254  262 PKTKELPKDSEEPAA--PSKSAEASTEKKEPDTESSPETSSEKSAPSLLSPVSKASIDKPLSSPDRD-PLSPKPKPQSPp 338
                          330
                   ....*....|....*
gi 767950714  1603 --FRV---RRVRASE 1612
Cdd:pfam13254  339 kdFRAnlrSREVPKD 353
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1382-1687 1.04e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 57.10  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1382 PAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLlkslfPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTR 1461
Cdd:PHA03307  172 AALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSS-----PISASASSPAPAPGRSAADDAGASSSDSSSSESSG 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1462 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEaqDGPPSPLSEASSGyfshSVSTATLSDALGP 1541
Cdd:PHA03307  247 CGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRER--SPSPSPSSPGSGP----APSSPRASSSSSS 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1542 ----GLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfRVRRVRASELRSFS 1617
Cdd:PHA03307  321 sresSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRP-TRRRARAAVAGRAR 399
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950714 1618 RMLAgdPGCSPGAEGNAPAPGAGGQALASDSEEADEVPewlrEGE-FVTVGAHKTGVVRYVGPADFQEGTW 1687
Cdd:PHA03307  400 RRDA--TGRFPAGRPRPSPLDAGAASGAFYARYPLLTP----SGEpWPGSPPPPPGRVRYGGLGDSRPGLW 464
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1447-1589 4.74e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 54.99  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1447 RIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP-PSPLSE 1520
Cdd:PRK07764  361 RMLLPSASDDErgllaRLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPaPAPAPA 440
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950714 1521 ASSGYFSHSVSTATLSDalgPGLDAAAPPGSMPTAPE----AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR 1589
Cdd:PRK07764  441 PPSPAGNAPAGGAPSPP---PAAAPSAQPAPAPAAAPeptaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
PHA03378 PHA03378
EBNA-3B; Provisional
1352-1643 6.70e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 54.69  E-value: 6.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1352 LIPSYSLGSNKGRWESQQDVSQ-TTVSRGIAPAPALSVSPqNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLF--PV 1428
Cdd:PHA03378  563 LLPAPGLGPLQIQPLTSPTTSQlASSAPSYAQTPWPVPHP-SQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRmqPI 641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1429 RDEKRGkRPSPlaHQPvPRIMVQSASPDIRVTRMEEAQPE-MGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVT----- 1502
Cdd:PHA03378  642 TFNVLV-FPTP--HQP-PQVEITPYKPTWTQIGHIPYQPSpTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGraqrp 717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1503 --AVTPAPEAQDGP-------------PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP 1567
Cdd:PHA03378  718 aaATGRARPPAAAPgrarppaaapgraRPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767950714 1568 PPPTAVPAEEPPGPQQLvsPGRERPDLEAPAPGSPFRVRRVRASeLRSFSRmlagdpGCSPGAEGNAPAPGAGGQA 1643
Cdd:PHA03378  798 PPPQAGPTSMQLMPRAA--PGQQGPTKQILRQLLTGGVKRGRPS-LKKPAA------LERQAAAGPTPSPGSGTSD 864
DUF3694 pfam12473
Kinesin protein; This domain family is found in eukaryotes, and is typically between 131 and ...
1157-1214 7.27e-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: 50.66  E-value: 7.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767950714  1157 VKAEASWDSAVHGCPQLSRGTPVDERLFLIVRVTVQ---LSHPAdmqlVLRKRICVNVHGR 1214
Cdd:pfam12473   91 YTIEGQWDSSLHNSLLLNRVTADGYRVYLTLAWDVVsekCAEPV----RFSMDTAVQIYPR 147
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
1426-1599 1.05e-06

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: 51.91  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1426 FPVRDEKRGKRP----------SPLAHQPVPRIMVQSASPDI-----RVTRMEEAQPEMGPDVLVQTMGAPALKICDKPA 1490
Cdd:pfam15822   16 SAVSNPKPGQPPqgwpgsnpwnNPSAPPAVPSGLPPSTAPSTvpfgpAPTGMYPSIPLTGPSPGPPAPFPPSGPSCPPPG 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1491 KvPSPPPVIAvtavTPAPEAQDGPPS-PLSEASSGYFSHS--VSTATL-------SDALGPGLDAAAPPGSMPTAPeaep 1560
Cdd:pfam15822   96 G-PYPAPTVP----GPGPIGPYPTPNmPFPELPRPYGAPTdpAAAAPSgpwgsmsSGPWAPGMGGQYPAPNMPYPS---- 166
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 767950714  1561 eaPISHP-PPPTAVPAEEPPGPQQLVSPGRERPDLEAPAP 1599
Cdd:pfam15822  167 --PGPYPaVPPPQSPGAAPPVPWGTVPPGPWGPPAPYPDP 204
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1353-1599 1.19e-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: 53.62  E-value: 1.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1353 IPSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPqnnhSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEk 1432
Cdd:pfam03154  148 IPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPS----PPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQ- 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1433 rgkrpSPLAhqpvPRIMVQSaSPDIRVTRMEEAQPEMGPdvlvQTMGAPALKICDKPakvpSPPPVIAvTAVTPAPEA-Q 1511
Cdd:pfam03154  223 -----STAA----PHTLIQQ-TPTLHPQRLPSPHPPLQP----MTQPPPPSQVSPQP----LPQPSLH-GQMPPMPHSlQ 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1512 DGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPP-------PPTAVPAEEPPGPQ-- 1582
Cdd:pfam03154  284 TGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPreqplppAPLSMPHIKPPPTTpi 363
                          250       260
                   ....*....|....*....|
gi 767950714  1583 -QLVSPGRER--PDLEAPAP 1599
Cdd:pfam03154  364 pQLPNPQSHKhpPHLSGPSP 383
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1381-1578 2.31e-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: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1381 APAPALSVSPQNNhSPDPGLSNlAASYLNPVKSFVP---QMPKLLK---SLFPVRDEKRGKRPSplAHQPVPRIMVQSas 1454
Cdd:pfam03154  348 APLSMPHIKPPPT-TPIPQLPN-PQSHKHPPHLSGPspfQMNSNLPpppALKPLSSLSTHHPPS--AHPPPLQLMPQS-- 421
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1455 pdirvtrMEEAQPEMGPDVLVQTMGAPALKICDKPA----KVPSPPPVIA---VTAVTPAPEAQDGPPSPLSEASSGYFS 1527
Cdd:pfam03154  422 -------QQLPPPPAQPPVLTQSQSLPPPAASHPPTsglhQVPSQSPFPQhpfVPGGPPPITPPSGPPTSTSSAMPGIQP 494
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767950714  1528 HSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPIShPPPPTAVPAEEP 1578
Cdd:pfam03154  495 PSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPES-PPPPPRSPSPEP 544
PHA03247 PHA03247
large tegument protein UL36; Provisional
1371-1643 4.21e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1371 VSQTTVSRGIAPAP-ALSVSPQNNHSPDPGLSNLA--ASYLNPVKSFVPQMPKLLKSLFPVRDEKRG---------KRPS 1438
Cdd:PHA03247 2788 VASLSESRESLPSPwDPADPPAAVLAPAAALPPAAspAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGsvapggdvrRRPP 2867
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1439 PLAHQPVPrimvqSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAV-TPAPEAQDGPPSP 1517
Cdd:PHA03247 2868 SRSPAAKP-----AAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPP 2942
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1518 LS----EASSGYFSHSVSTATLSdALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPA-----------EEP-PGP 1581
Cdd:PHA03247 2943 LApttdPAGAGEPSGAVPQPWLG-ALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGHSLSRvsswasslalhEETdPPP 3021
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950714 1582 QQLVSPGRERPDLEAPAPGSPFRVRRVRaSELRSFSRmLAGDPGCSPGAEGNAPAPGAGGQA 1643
Cdd:PHA03247 3022 VSLKQTLWPPDDTEDSDADSLFDSDSER-SDLEALDP-LPPEPHDPFAHEPDPATPEAGARE 3081
PHA03247 PHA03247
large tegument protein UL36; Provisional
1379-1655 4.28e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1379 GIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFV-PQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqsASPDI 1457
Cdd:PHA03247 2493 GAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPVhPRMLTWIRGLEELASDDAGDPPPPLPPAAPP------AAPDR 2566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1458 RVTRMEEAQPEMGPDVLVQTM--GAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATL 1535
Cdd:PHA03247 2567 SVPPPRPAPRPSEPAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTV 2646
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1536 SDALGPGLDAAAPPGSM---------PTAPEAEPEAP--------------ISHPPPPTAVPAEEP-------PGPQQLV 1585
Cdd:PHA03247 2647 PPPERPRDDPAPGRVSRprrarrlgrAAQASSPPQRPrrraarptvgsltsLADPPPPPPTPEPAPhalvsatPLPPGPA 2726
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767950714 1586 SPGRERPDLE-APAPGSPFRVRRVRASELRSFSRMLAGDPGCS--PGAEGNAPAPGAGGQALASDSEEADEVP 1655
Cdd:PHA03247 2727 AARQASPALPaAPAPPAVPAGPATPGGPARPARPPTTAGPPAPapPAAPAAGPPRRLTRPAVASLSESRESLP 2799
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1494-1656 4.35e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1494 SPPPVIAVTAVTPAPEAQdgPPSPLSEASSGYFSHSVSTATLSDALGPgldAAAPPGSMPTAPEAEPEA-------PISH 1566
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAA--APAAAAPAPAAPPAAPAAAPAAAAAARA---VAAAPARRSPAPEALAAArqasargPGGA 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1567 PPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVR-RVRASELRSFSRMLAGDPGcSPGAEGNAPAPGAGGQALA 1645
Cdd:PRK12323  448 PAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAaPAPADDDPPPWEELPPEFA-SPAPAQPDAAPAGWVAESI 526
                         170
                  ....*....|.
gi 767950714 1646 SDSEEADEVPE 1656
Cdd:PRK12323  527 PDPATADPDDA 537
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1490-1611 8.61e-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: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1490 AKVPSPPPVIAVT---AVTPAPEAQDGPPSPLSEASSG-----YFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPE 1561
Cdd:NF040712  200 ATVPRLAREPADArpeEVEPAPAAEGAPATDSDPAEAGtpddlASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGE 279
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767950714 1562 APIS---HPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRAS 1611
Cdd:NF040712  280 PPAPgaaETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPPPAPKPKRRRRRAS 332
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1434-1652 8.65e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 50.64  E-value: 8.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1434 GKRPSPLAHQPVPRIMVQSASPdiRVTRMEEAQPEMGPDVLVQTmGAPALKICDKPAKvPSPPPViavtAVTPAPEAQDG 1513
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAAAP--AAAAPAPAAPPAAPAAAPAA-AAAARAVAAAPAR-RSPAPE----ALAAARQASAR 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1514 PPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEP-PGPQQL-------- 1584
Cdd:PRK12323  443 GPGGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFAsPAPAQPdaapagwv 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1585 ---------VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGAG------GQALASDSE 1649
Cdd:PRK12323  523 aesipdpatADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARlpvrglAQQLARQSE 602

                  ...
gi 767950714 1650 EAD 1652
Cdd:PRK12323  603 LAG 605
PHA03247 PHA03247
large tegument protein UL36; Provisional
1529-1637 1.04e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.71  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1529 SVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHP----------------------PPPTAVPAEEPPGPQQLVS 1586
Cdd:PHA03247 2490 FAAGAAPDPGGGGPPDPDAPPAPSRLAPAILPDEPVGEPvhprmltwirgleelasddagdPPPPLPPAAPPAAPDRSVP 2569
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767950714 1587 PGRERPDLEAPAPGSpfRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAP 1637
Cdd:PHA03247 2570 PPRPAPRPSEPAVTS--RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLP 2618
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1530-1688 1.08e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1530 VSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPFRVRRVR 1609
Cdd:PRK07764  393 APAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAA 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1610 ASEL--RSFSRMLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLREGEFVTVGAhktgVVRYVGPADFQEGTW 1687
Cdd:PRK07764  473 APEPtaAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI----LLPEATVLGVRGDTL 548

                  .
gi 767950714 1688 V 1688
Cdd:PRK07764  549 V 549
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
404-478 1.11e-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: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714  404 KEHTLIGSANSQDIQLCGMGILPEHCIIDITsEGQVMLTPQKNTR-TFVNGSSVSSPIQLHHGDRILWGNNHF-FRL 478
Cdd:COG1716    20 GGPLTIGRAPDNDIVLDDPTVSRRHARIRRD-GGGWVLEDLGSTNgTFVNGQRVTEPAPLRDGDVIRLGKTELrFRL 95
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
1477-1578 1.30e-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: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1477 TMGAPALKICDkPAKVPSPPPVIAVTAVTPAPEAQDGPPSPlseassgyfshsvsTATLSDALGPGldaAAPPGSMPTAP 1556
Cdd:pfam07174   30 AVALPAVAHAD-PEPAPPPPSTATAPPAPPPPPPAPAAPAP--------------PPPPAAPNAPN---APPPPADPNAP 91
                           90       100
                   ....*....|....*....|..
gi 767950714  1557 EAEPEAPISHPPPPTAVPAEEP 1578
Cdd:pfam07174   92 PPPPADPNAPPPPAVDPNAPEP 113
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
1451-1603 1.46e-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: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1451 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV 1530
Cdd:pfam03154  142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGP-----TPSAPSVPPQGSPATSQ 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1531 STATLSDALGP-GLDAAAPPGSMPTAPEAEPE-APISHPPPPTAVPAEE----------PPGPQQLVS-PgrerPDLEAP 1597
Cdd:pfam03154  217 PPNQTQSTAAPhTLIQQTPTLHPQRLPSPHPPlQPMTQPPPPSQVSPQPlpqpslhgqmPPMPHSLQTgP----SHMQHP 292

                   ....*.
gi 767950714  1598 APGSPF 1603
Cdd:pfam03154  293 VPPQPF 298
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
1346-1602 2.69e-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: 48.27  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1346 SGSRQDLI-PSYSLGSNKGRWESQQDVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLaasylNPVKSFVPQMPKLLKS 1424
Cdd:pfam15279   62 AGSSAQLItPDLWLSDCRRKSASPASTRSESVSPGPSSSASPSSSPTSSNSSKPLISVA-----SSSKLLAPKPHEPPSL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1425 LFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKicdKPAKVPSPPPV----IA 1500
Cdd:pfam15279  137 PPPPLPPKKGRRHRPGLHPPLGRPPGSPPMSMTPRGLLGKPQQHPPPSPLPAFMEPSSMP---PPFLRPPPSIPqpnsPL 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1501 VTAVTPAPEAQDGPPSPLSEASSGY----FS--HSVSTATLSdalGPgldaaaPPGSMPTAPEAEPeaPISHPPPPtavP 1574
Cdd:pfam15279  214 SNPMLPGIGPPPKPPRNLGPPSNPMhrppFSphHPPPPPTPP---GP------PPGLPPPPPRGFT--PPFGPPFP---P 279
                          250       260
                   ....*....|....*....|....*...
gi 767950714  1575 AEEPPGPQQLvspgreRPDLEAPAPGSP 1602
Cdd:pfam15279  280 VNMMPNPPEM------NFGLPSLAPLVP 301
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1465-1647 2.92e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 49.08  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1465 AQPEMGPdVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLD 1544
Cdd:PRK07003  395 AVPAVTA-VTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPAD 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1545 A---AAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQqlvspGRERPDleAPAPGSPfrvrrvraselrsfsrmla 1621
Cdd:PRK07003  474 SgsaSAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPA-----AASRED--APAAAAP------------------- 527
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767950714 1622 gdpgcsPGAEGNAPAPGA-------GGQALASD 1647
Cdd:PRK07003  528 ------PAPEARPPTPAAaapaaraGGAAAALD 554
PHA03377 PHA03377
EBNA-3C; Provisional
1407-1600 3.15e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 48.90  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1407 YLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDirvtRMEEAQ--PEM-GP-DVLVQTMGAPA 1482
Cdd:PHA03377  392 YIDPNMEPVQQRPVMFVSRVPWRKPRTLPWPTPKTHPVKRTLVKTSGRSD----EAEQAQstPERpGPsDQPSVPVEPAH 467
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1483 LKICDKP-AKVPSPPPVIAVTAVTPAPeaqdgPPSPLSEASSGYFSHSV-------STATLSDALGPGLDAAAP------ 1548
Cdd:PHA03377  468 LTPVEHTtVILHQPPQSPPTVAIKPAP-----PPSRRRRGACVVYDDDIievidveTTEEEESVTQPAKPHRKVqdgfqr 542
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767950714 1549 PGSMPTAPEAEPEAPISHPPPPTAVPAEEPP--GPQQLVSPGRERPDLEAPAPG 1600
Cdd:PHA03377  543 SGRRQKRATPPKVSPSDRGPPKASPPVMAPPstGPRVMATPSTGPRDMAPPSTG 596
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
1489-1602 4.56e-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: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1489 PAKVPSPPPVIAVTAVTPAP----EAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPI 1564
Cdd:pfam06346   18 GACIPTPPPLPGGGGPPPPPplpgSAAIPPPPPL----------------------PGGTSIPPPPPLPGAASIPPPPPL 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714  1565 SH----PPPP-----TAVPAEEPPGPQqlvSPGRERPdlEAPAPGSP 1602
Cdd:pfam06346   76 PGstgiPPPPplpggAGIPPPPPPLPG---GAGVPPP--PPPLPGGP 117
PHA03247 PHA03247
large tegument protein UL36; Provisional
1492-1655 5.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1492 VPSPPPVIAVTAVTPaPEAQDG--PPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPISHPPP 1569
Cdd:PHA03247  254 APAPPPVVGEGADRA-PETARGatGPPPPPEAAA-----------------PNGAAAPPDGVWGAALAGAPLALPAPPDP 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1570 PTAVPAEEP----------------PGPQQLVS---PGRERP---------DLEA---PAPGSPFRVRRVRASELRS--F 1616
Cdd:PHA03247  316 PPPAPAGDAeeeddedgamevvsplPRPRQHYPlgfPKRRRPtwtppssleDLSAgrhHPKRASLPTRKRRSARHAAtpF 395
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767950714 1617 SRMLAGD--PGCSPGAEGNAPAPGAGGQALASDSEEADEVP 1655
Cdd:PHA03247  396 ARGPGGDdqTRPAAPVPASVPTPAPTPVPASAPPPPATPLP 436
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1498-1655 5.24e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1498 VIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEE 1577
Cdd:PRK07764  584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714 1578 PPGPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADEVP 1655
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPP--AGQADDPAAQPPQAAQGASAPSPAADDPV 739
PHA03369 PHA03369
capsid maturational protease; Provisional
1367-1600 6.91e-05

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 47.69  E-value: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1367 SQQDVSQTTVSRGI--APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLF------PVRDEKRGKRPS 1438
Cdd:PHA03369  393 SVPARSPMTAYPPVpqFCGDPGLVSPYNPQSPGTSYGPEPVGPVPPQPTNPYVMPISMANMVypghpqEHGHERKRKRGG 472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1439 PL------AHQPVPRIMVQ---SASPDIRVTRMEEAQPEM---GPDVLVQTMGAPALKICDKPA-----KVPSPPPVIAV 1501
Cdd:PHA03369  473 ELkeelieTLKLVKKLKEEqesLAKELEATAHKSEIKKIAeseFKNAGAKTAAANIEPNCSADAaapatKRARPETKTEL 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1502 TAVTPAPEAQDGPPSPLseassgyFSHSVSTATLSDALGPGLDAAA----------------PPGSMPTAPEAEPEAPIS 1565
Cdd:PHA03369  553 EAVVRFPYQIRNMESPA-------FVHSFTSTTLAAAAGQGSDTAEalagaietlltqasaqPAGLSLPAPAVPVNASTP 625
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767950714 1566 HPPPPTAVPAEEPPgpqqlvsPGRERPDLEAPAPG 1600
Cdd:PHA03369  626 ASTPPPLAPQEPPQ-------PGTSAPSLETSLPQ 653
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
1488-1652 8.46e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 47.40  E-value: 8.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1488 KP-AKVPSPPPVIAVTAVTPAPEAQDgpPSPLSEASSgyfshsvstatlsdalgPGLDAAAPPGSMPTAPEAEPEAPish 1566
Cdd:PRK14951  365 KPaAAAEAAAPAEKKTPARPEAAAPA--AAPVAQAAA-----------------APAPAAAPAAAASAPAAPPAAAP--- 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1567 pPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPGSPfrvrrvrasELRSFSRMLAGDPGCSPGAEGNAPAPGAggqALAS 1646
Cdd:PRK14951  423 -PAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAP---------ETVAIPVRVAPEPAVASAAPAPAAAPAA---ARLT 489

                  ....*.
gi 767950714 1647 DSEEAD 1652
Cdd:PRK14951  490 PTEEGD 495
bMERB_dom pfam12130
Bivalent Mical/EHBP Rab binding domain; A variety of different effector proteins interact ...
1035-1079 1.38e-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: 1.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 767950714  1035 LTKRQEYLDQQLQKLVSKRD--KTEDDADREAQLLEMRLTLTEERNA 1079
Cdd:pfam12130   66 LEERQARLEQELRELMSKPDwlKTEEDKQREEELLEELVEIVEQRDA 112
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
1381-1602 2.18e-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: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNnhspdpglsnlaasylnPVKSFVPQMPKLLKSLFPvRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVT 1460
Cdd:NF033839  294 APKPGMQPSPQP-----------------EKKEVKPEPETPKPEVKP-QLEKPKPEVKPQPEKPKPEVKPQLETPKPEVK 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1461 RMEEA-QPEMGPDvlvqtmgaPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASsgyfshsvstatlsdal 1539
Cdd:NF033839  356 PQPEKpKPEVKPQ--------PEKPKPEVKPQPETPKPEVKPQPEKPKPEVKPQPEKPKPEVK----------------- 410
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714 1540 gPGLDAAAP---PGSMPTAPEAEPEapishPPPPTAVPAEEPPGPQQLVSPGRERPDLEA-PAPGSP 1602
Cdd:NF033839  411 -PQPEKPKPevkPQPEKPKPEVKPQ-----PEKPKPEVKPQPEKPKPEVKPQPETPKPEVkPQPEKP 471
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1436-1657 3.21e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1436 RPSPLAhqpvPRIMVQSASPDIRVTRM---EEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPPVIAVTAVTPAPeaqD 1512
Cdd:PRK07003  411 APKAAA----AAAATRAEAPPAAPAPPataDRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPAS---D 483
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1513 GPPSPLSEASSgyfshsvSTATLSDALGPGLDAAAPPGSMPTAPEAEPEA-PISHPPPPTavPAEEPPGPQQ-------- 1583
Cdd:PRK07003  484 APPDAAFEPAP-------RAAAPSAATPAAVPDARAPAAASREDAPAAAApPAPEARPPT--PAAAAPAARAggaaaald 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1584 -------LVSPGRERPDLEAPAPGSPfrvrrVRASELRSFSRMLAGDPgcSPGAEGNAPAPGAGGQALASDSEEADE-VP 1655
Cdd:PRK07003  555 vlrnagmRVSSDRGARAAAAAKPAAA-----PAAAPKPAAPRVAVQVP--TPRARAATGDAPPNGAARAEQAAESRGaPP 627

                  ..
gi 767950714 1656 EW 1657
Cdd:PRK07003  628 PW 629
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
1490-1655 3.34e-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: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1490 AKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSgyfshSVSTATLSDALGPgldaaaPPGSMPTAPEAEPEAP------ 1563
Cdd:PLN03209  336 ADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPR-----PLSPYTAYEDLKP------PTSPIPTPPSSSPASSksvdav 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1564 --------ISHPPPPTAVPAEEP-PGPQQL---VSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAE 1631
Cdd:PLN03209  405 akpaepdvVPSPGSASNVPEVEPaQVEAKKtrpLSPYARYEDLKPPTSPSPTAPTGVSPSVSSTSSVPAVPDTAPATAAT 484
                         170       180
                  ....*....|....*....|....
gi 767950714 1632 GNAPAPGAGGQALASDSEEADEVP 1655
Cdd:PLN03209  485 DAAAPPPANMRPLSPYAVYDDLKP 508
dnaA PRK14086
chromosomal replication initiator protein DnaA;
1489-1641 3.88e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.20  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1489 PAKVPSPPPviavtavTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAP----------PGSMP--- 1553
Cdd:PRK14086   90 PSAGEPAPP-------PPHARRTSEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPaypayqqrpePGAWPraa 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1554 ------------------TAPEAEPEAPISHPPPPTAVPAEEPPGPQQ-------LVSPGRERPDLEAPAPGSPFRVRRV 1608
Cdd:PRK14086  163 ddygwqqqrlgfpprapyASPASYAPEQERDREPYDAGRPEYDQRRRDydhprpdWDRPRRDRTDRPEPPPGAGHVHRGG 242
                         170       180       190
                  ....*....|....*....|....*....|....
gi 767950714 1609 R-ASELRSFSRMLAGDPGCSPGAEGNAPAPGAGG 1641
Cdd:PRK14086  243 PgPPERDDAPVVPIRPSAPGPLAAQPAPAPGPGE 276
KLF9_13_N-like cd21975
Kruppel-like factor (KLF) 9, KLF13, KLF14, KLF16, and similar proteins; Kruppel/Krueppel-like ...
1462-1598 4.88e-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: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1462 MEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSPPpviAVTAVTPAPEAQDgPPSPLSEASS-----------GYFSHSV 1530
Cdd:cd21975    12 ISAGAVVHGVRPDPEGAGLAAGLDVRATREVAKGP---GPPGPAWKPDGAD-SPGLVTAAPHllaanvlaplrGPSVEGS 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767950714 1531 STATLSDALGPGLDAAAPPGSM-PTAPEAE---PEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPA 1598
Cdd:cd21975    88 SLESGDADMGSDSDVAPASGAAaSTSPESSsdaASSPSPLSLLHPGEAGLEPERPRPRVRRGVRRRGVTPAA 159
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1480-1655 5.24e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.84  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1480 APALKICDKPAKVPSPPPVIAVtavtPAPEAQdgpPSPLSEASSGYFSHSVSTATLSdalgpgldAAAPPGSMPTAPeAE 1559
Cdd:PRK07003  359 EPAVTGGGAPGGGVPARVAGAV----PAPGAR---AAAAVGASAVPAVTAVTGAAGA--------ALAPKAAAAAAA-TR 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1560 PEAPISHPPPPTAVPAEEPPGPQQLVSPGrerpdlEAPAPGSPFRVRRVRASELRSFSRMLAGDPGCSPGAEGNAPAPGA 1639
Cdd:PRK07003  423 AEAPPAAPAPPATADRGDDAADGDAPVPA------KANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRA 496
                         170
                  ....*....|....*.
gi 767950714 1640 GGQALASDSEEADEVP 1655
Cdd:PRK07003  497 AAPSAATPAAVPDARA 512
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1381-1599 5.61e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.87  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1381 APAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPrimvqSASPdIRVT 1460
Cdd:PRK12323  389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAP-----AAAP-AAAA 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1461 RMEEAQPEmgpdvlvqtmGAPALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSDALG 1540
Cdd:PRK12323  463 RPAAAGPR----------PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767950714 1541 PGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQlVSPGrERPDLEAPAP 1599
Cdd:PRK12323  533 DPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD-MFDG-DWPALAARLP 589
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1433-1604 6.08e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1433 RGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGPDVLVQTMGAPalkiCDKPAKVPSPPPVIAVTAVTPAPEAQD 1512
Cdd:PHA03307  764 VPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAA----SRTASKRKSRSHTPDGGSESSGPARPP 839
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1513 GP-PSPLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPgreR 1591
Cdd:PHA03307  840 GAaARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGP---M 916
                         170
                  ....*....|...
gi 767950714 1592 PdLEAPAPGSPFR 1604
Cdd:PHA03307  917 P-PGGPDPRGGFR 928
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
1500-1599 7.25e-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: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1500 AVTAVTPAPEAQDGPPSPLseassgyfshsvstatlsdalgPGLDAAAPPgsMPTAPEAEPEAPISHPPPPTAVPAEEPP 1579
Cdd:pfam07174   28 AVAVALPAVAHADPEPAPP----------------------PPSTATAPP--APPPPPPAPAAPAPPPPPAAPNAPNAPP 83
                           90       100
                   ....*....|....*....|
gi 767950714  1580 GPQQLVSPGRERPDLEAPAP 1599
Cdd:pfam07174   84 PPADPNAPPPPPADPNAPPP 103
FHA_RADIL cd22733
forkhead associated (FHA) domain found in Ras-associating and dilute domain-containing protein ...
396-476 8.81e-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: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  396 NELLVYYL-KEHTLIG---SANSQDIQLCGMGILPEHCII------DITSEGQVMLTPQKNTRTFVNGSSVSSPIQLHHG 465
Cdd:cd22733    18 HDCLVYLLnREQHTVGqetPSSKPNISLSAPDILPLHCTIrrvrlpKHRSEEKLVLEPIPGAHVSVNFSEVERTTLLRHG 97
                          90
                  ....*....|.
gi 767950714  466 DRILWGNNHFF 476
Cdd:cd22733    98 DLLSFGAYYLF 108
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
1536-1620 8.84e-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: 43.84  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1536 SDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGR--ERPDLEAPAPGSPFRVRRVRA-SE 1612
Cdd:NF041121   22 PSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPppPGPAGAAPGAALPVRVPAPPAlPN 101

                  ....*...
gi 767950714 1613 LRSFSRML 1620
Cdd:NF041121  102 PLELARAL 109
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1437-1598 1.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1437 PSPLAHQPVPRImvqSASPDIRVTRMEEAQPEmGPDVLVQTMGAPAlkicdkPAKVPSPPPVIAVTAVTPAPEAQDGPPS 1516
Cdd:PRK07764  651 EHHPKHVAVPDA---SDGGDGWPAKAGGAAPA-APPPAPAPAAPAA------PAGAAPAQPAPAPAATPPAGQADDPAAQ 720
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1517 PLSEASSGYFSHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEA 1596
Cdd:PRK07764  721 PPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRD 800

                  ..
gi 767950714 1597 PA 1598
Cdd:PRK07764  801 AE 802
PHA03247 PHA03247
large tegument protein UL36; Provisional
1370-1613 1.12e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1370 DVSQTTVSRGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVksfvPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIM 1449
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPP----DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1450 VQSASPdIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKP-AKVPSPPPVIAVTAvTPAPEAQDGPPSPLSEASSGYFSH 1528
Cdd:PHA03247 2937 PRPQPP-LAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrFRVPQPAPSREAPA-SSTPPLTGHSLSRVSSWASSLALH 3014
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1529 SVST---ATLSDALGP-----GLDAAAPPGSMPTAPEAE--------PEAPISHPPPPTAVPAEEPPGPQQLVSPgrerP 1592
Cdd:PHA03247 3015 EETDpppVSLKQTLWPpddteDSDADSLFDSDSERSDLEaldplppePHDPFAHEPDPATPEAGARESPSSQFGP----P 3090
                         250       260
                  ....*....|....*....|.
gi 767950714 1593 DLEAPAPGSPFRVRRVRASEL 1613
Cdd:PHA03247 3091 PLSANAALSRRYVRSTGRSAL 3111
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
1434-1660 1.35e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 43.70  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1434 GKRPSPLAhqPVPRI---MVqsaspdirVTRM-------EEAQPEMGPDVLVQTMGAPALKicDKPAKVPSPPPVIAVTA 1503
Cdd:PRK07994  335 GRKDLPLA--PDRRMgveMT--------LLRMlafhpaaPLPEPEVPPQSAAPAASAQATA--APTAAVAPPQAPAVPPP 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1504 VTPAPEAQdgPPSPLSEAssgyfshsvsTATLSDALgPGLDAAAPPgsmPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQ 1583
Cdd:PRK07994  403 PASAPQQA--PAVPLPET----------TSQLLAAR-QQLQRAQGA---TKAKKSEPAAASRARPVNSALERLASVRPAP 466
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714 1584 LVSPgrerpdlEAPAPGSPFRVRRVRASElrsfsrmLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPEWLRE 1660
Cdd:PRK07994  467 SALE-------KAPAKKEAYRWKATNPVE-------VKKEPVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAL 529
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
1392-1609 1.58e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 43.05  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1392 NNHSPDPGLSNLAASylNPVKSFVPQMPKLLKSLFPVRDEKRGKRPSPLAHQPVPRIMVQSASPDIRVTRMEEAQPEMGP 1471
Cdd:PRK12727   30 SNRRTAEGIEIVAAS--NYDEELVQRALETARSDTPATAAAPAPAPQAPTKPAAPVHAPLKLSANANMSQRQRVASAAED 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1472 DVLVQTMGAPALKICDKPAKVP-----SPPPVIAVTAVTPAPEAQDGPPSPLSEASSGYFSHSVSTATLSD-ALGPGLDA 1545
Cdd:PRK12727  108 MIAAMALRQPVSVPRQAPAAAPvraasIPSPAAQALAHAAAVRTAPRQEHALSAVPEQLFADFLTTAPVPRaPVQAPVVA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1546 AAPPGSMPTAPEAEPEAPISH--------------PPPPTAVPAEEPP---GPQQLVSPGRERpdLEAPAPGSPFRVRRV 1608
Cdd:PRK12727  188 APAPVPAIAAALAAHAAYAQDddeqldddgfdlddALPQILPPAALPPivvAPAAPAALAAVA--AAAPAPQNDEELKQL 265

                  .
gi 767950714 1609 R 1609
Cdd:PRK12727  266 R 266
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1496-1602 1.68e-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: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1496 PPVIAVTAV-TPAPEAQDGPPSPLSEASSGYF---SHSVSTATLSDALGPGLDAAAPPGSMPTAPEAEPEAPISHPPPPT 1571
Cdd:NF040712  194 RPLRPLATVpRLAREPADARPEEVEPAPAAEGapaTDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEA 273
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767950714 1572 AVPAEEPPGPQQLVSPGRERPDLEAPAPGSP 1602
Cdd:NF040712  274 TRDAGEPPAPGAAETPEAAEPPAPAPAAPAA 304
half-pint TIGR01645
poly-U binding splicing factor, half-pint family; The proteins represented by this model ...
1489-1656 1.82e-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: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1489 PAKVPSPPPVIAV-----TAVTPAPEAQDGPPSP-LSEASSGYFSHSVSTATLSDAL-GPGLDAAAPPGSMP-TAPEAEP 1560
Cdd:TIGR01645  291 PATVSAIPAAAAVaaaaaTAKIMAAEAVAGAAVLgPRAQSPATPSSSLPTDIGNKAVvSSAKKEAEEVPPLPqAAPAVVK 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714  1561 ----EAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEApAPGSPFRVRRVRASELRSFSRMLAGDP--GCSPGAEGNA 1634
Cdd:TIGR01645  371 pgpmEIPTPVPPPGLAIPSLVA--PPGLVAPTEINPSFLA-SPRKKMKREKLPVTFGALDDTLAWKEPskEDQTSEDGKM 447
                          170       180
                   ....*....|....*....|...
gi 767950714  1635 PA-PGAGGQALASDSEEADEVPE 1656
Cdd:TIGR01645  448 LAiMGEAAAALALEPKKKKKEKE 470
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
1502-1599 1.83e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.87  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1502 TAVTPAPEAQDGPPsplseassgyfshsvsTATLSDALGPGLDAAAPPGSMPTA--PEAEPEAPISHPPPPTAVPAEEPP 1579
Cdd:PRK14950  358 ALLVPVPAPQPAKP----------------TAAAPSPVRPTPAPSTRPKAAAAAniPPKEPVRETATPPPVPPRPVAPPV 421
                          90       100
                  ....*....|....*....|....*...
gi 767950714 1580 GPQQ--------LVSPGRERPDLEAPAP 1599
Cdd:PRK14950  422 PHTPesapkltrAAIPVDEKPKYTPPAP 449
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
304-380 1.93e-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: 1.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767950714  304 IRDLREEVEKLREQLTKAE--AMKSPELKDRLEESEKLIQEMTVTWEEKLRKTEEIAQERQKQLESLGISLQSSGIKVG 380
Cdd:COG5493    36 LEELLERLEKLEEQMRKWEeqLRKLEEEIKKLREQVRKLEEDVKRLEEQERKLEEAMAEHSELREELMKLIKRLERSIG 114
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1539-1656 2.25e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1539 LGPGLDAAAPPGSMPTAPEAEPEApiSHPPPPTAVPAEEPPGPqqlvsPGRERPdLEAPAPGSPFRVRRVRASELRSFSR 1618
Cdd:PRK07764  385 LGVAGGAGAPAAAAPSAAAAAPAA--APAPAAAAPAAAAAPAP-----AAAPQP-APAPAPAPAPPSPAGNAPAGGAPSP 456
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767950714 1619 MLAGDPGCSPGAEGNAPAPGAGGQALASDSEEADEVPE 1656
Cdd:PRK07764  457 PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAP 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
304-368 2.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767950714  304 IRDLREEVEKLREQLTKAEAMKS--PELKDRLEESEKLIQEMtvtwEEKLRKTEEIAQERQKQLESL 368
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKRKL----EEKIRELEERIEELKKEIEEL 278
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1480-1645 3.66e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1480 APALKICDKPAKVPSPPPVIAVTAVTPAPEAQDGP--PSPLSEASSGYFSHSVSTATLSDALGPGldAAAPPGSMPTAPE 1557
Cdd:PHA03307  776 EPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADaaSRTASKRKSRSHTPDGGSESSGPARPPG--AAARPPPARSSES 853
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1558 AEPEAPISHPPPPTAVPAEEPPGPQQLVSPGRERPDLEAPAPG-SPFRVRRVRASELRSFSRMLAGDP---GC---SPGA 1630
Cdd:PHA03307  854 SKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPpAGAPAPRPRPAPRVKLGPMPPGGPdprGGfrrVPPG 933
                         170
                  ....*....|....*
gi 767950714 1631 EGNAPAPGAggQALA 1645
Cdd:PHA03307  934 DLHTPAPSA--AALA 946
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
547-696 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 767950714  547 LNSLEQQHE--EEKRSALERQRlmyeHELEQLRRRLSPEKQNCRSMDRFSFHS---PSAQQRLRQWAEEREATLNNS--L 619
Cdd:COG4913   612 LAALEAELAelEEELAEAEERL----EALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELERLDASSddL 687
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767950714  620 MRLREQIVKANLLVREANYIAEELDKRteykvtlqipASSLDANRKR-GSLLSEPAIQVRRKGKGKQIWSLEKLDNRL 696
Cdd:COG4913   688 AALEEQLEELEAELEELEEELDELKGE----------IGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERF 755
flhF PRK06995
flagellar biosynthesis protein FlhF;
1543-1637 8.50e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 40.72  E-value: 8.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1543 LDAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPpgPQQLVSPGRERPDLEAPAPGSPFRVRRVRASELRSFSRMLAG 1622
Cdd:PRK06995   48 LAALAPPAAAAPAAAQPPPAAAPAAVSRPAAPAAEP--APWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125
                          90
                  ....*....|....*
gi 767950714 1623 DPGCSPGAEGNAPAP 1637
Cdd:PRK06995  126 ENAARRLARAAAAAP 140
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
1378-1599 9.15e-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: 40.60  E-value: 9.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1378 RGIAPAPALSVSPQNNHSPDPGLSNLAASYLNPVKSFVPQMPKLLKSLFPVRDE-------KRGKRPSPLAHQPVPRIMV 1450
Cdd:COG3266   109 LLRAAALLLLKLLLLLLTLLLLVLLLLLALLLALLLDLPLLTLLIVLPLLEEQLlllalqdIQGTLQALGAVAALLGLRK 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767950714 1451 QSASPDIRVTRMEEAQPEMGPDVLVQTMGAPALKICDKPAKVPSP---PPVIAVTAVTPAPEAQDGPPSPLSEASSGYFS 1527
Cdd:COG3266   189 AEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAagaAEVLTARLVLLLLIIGSALKAPSQASSASAPA 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767950714 1528 HSVSTATLSDALGPGldAAAPPGSMPTAPEAEPEAPISHPPPPTAVPAEEPPGPQQLVSP--GRERPDLEAPAP 1599
Cdd:COG3266   269 TTSLGEQQEVSLPPA--VAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKpvVTETAAPAAPAP 340
 
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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