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Conserved domains on  [gi|44889014|sp|P34531|]
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RecName: Full=CAP-Gly domain-containing linker protein 1 homolog

Protein Classification

CAP-Gly domain-containing protein( domain architecture ID 10472968)

cytoskeleton-associated protein (CAP)-Gly domain-containing protein similar to Saccharomyces cerevisiae nuclear fusion protein BIK1, a protein required for microtubule function during mating and mitosis

CATH:  2.30.30.190
Gene Ontology:  GO:0031122|GO:0008017

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
21-85 1.79e-23

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: 94.39  E-value: 1.79e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 44889014    21 IGRLVDVVNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIFAPIFRV 85
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
PTZ00121 super family cl31754
MAEBL; Provisional
364-793 9.10e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   364 VKQKAPSKHQlmMEQLKAsiEAEKTKPKKEIKSRVSLLPPPAPKAPQKENKEGGEMTETPRRTITKTPLKTVNAKAKTsp 443
Cdd:PTZ00121 1307 AKKKAEEAKK--ADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-- 1380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   444 tppvERQKKERKPLYVAPPAKERVEKEKKipsKPVVSPPTTAEKKPVVSSIPSTSSASKGPfptssfaggklQGPRKTSS 523
Cdd:PTZ00121 1381 ----DAAKKKAEEKKKADEAKKKAEEDKK---KADELKKAAAAKKKADEAKKKAEEKKKAD-----------EAKKKAEE 1442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   524 SSTTTSAKKQKNPPIDEKEKLSRLQHSTHAFEATLIVMNRINEDNERKLgniSEQYEKKVSEL---GDLKKMLDEARKKF 600
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAkkaAEAKKKADEAKKAE 1519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   601 E-EDVEQMKNSNQQVIRNHANAVESLQKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKVVACLDEKISEAEKQ 679
Cdd:PTZ00121 1520 EaKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   680 CEQLNVDKKVLQAALANDCDHRNQMLTKEISSLQTALEMKSAEMKELRqKNQNLSLQVDEIPLKELEISKW----KHKSN 755
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKaeedKKKAE 1678
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 44889014   756 EYKQMLDQKINGEKILVQQIEDLRR-KQIHDEEEKEAMK 793
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKK 1717
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
21-85 1.79e-23

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: 94.39  E-value: 1.79e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 44889014    21 IGRLVDVVNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIFAPIFRV 85
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
21-86 3.68e-20

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: 84.94  E-value: 3.68e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 44889014     21 IGRLVDVVNVGK-GFLRYVGPIHGKDGMFCGIELLEPN-GKHDGTFQGVSYFIATPYHGIFAPIFRVT 86
Cdd:smart01052   1 VGDRVEVGGGGRrGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
28-79 1.70e-05

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: 48.53  E-value: 1.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 44889014  28 VNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIF 79
Cdd:COG5244  12 LGDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
PTZ00121 PTZ00121
MAEBL; Provisional
364-793 9.10e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   364 VKQKAPSKHQlmMEQLKAsiEAEKTKPKKEIKSRVSLLPPPAPKAPQKENKEGGEMTETPRRTITKTPLKTVNAKAKTsp 443
Cdd:PTZ00121 1307 AKKKAEEAKK--ADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-- 1380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   444 tppvERQKKERKPLYVAPPAKERVEKEKKipsKPVVSPPTTAEKKPVVSSIPSTSSASKGPfptssfaggklQGPRKTSS 523
Cdd:PTZ00121 1381 ----DAAKKKAEEKKKADEAKKKAEEDKK---KADELKKAAAAKKKADEAKKKAEEKKKAD-----------EAKKKAEE 1442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   524 SSTTTSAKKQKNPPIDEKEKLSRLQHSTHAFEATLIVMNRINEDNERKLgniSEQYEKKVSEL---GDLKKMLDEARKKF 600
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAkkaAEAKKKADEAKKAE 1519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   601 E-EDVEQMKNSNQQVIRNHANAVESLQKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKVVACLDEKISEAEKQ 679
Cdd:PTZ00121 1520 EaKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   680 CEQLNVDKKVLQAALANDCDHRNQMLTKEISSLQTALEMKSAEMKELRqKNQNLSLQVDEIPLKELEISKW----KHKSN 755
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKaeedKKKAE 1678
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 44889014   756 EYKQMLDQKINGEKILVQQIEDLRR-KQIHDEEEKEAMK 793
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKK 1717
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
538-793 2.30e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    538 IDE-KEKLSRLQHSTHAFEATLIVMnrinednERKLGNISEQYEKKVSELGDLKKMLDEARKKFEEDVEQMKNSNQQVIR 616
Cdd:TIGR02168  679 IEElEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    617 NHANAVESL-QKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKvvacLDEKISEAEKQCEQLNVDkkvlqaalA 695
Cdd:TIGR02168  752 LSKELTELEaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEE--------A 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    696 NDCDHRNQMLTKEISSLQTALEMKSAEMKELRQKNQNLSLQVD--EIPLKELEiSKWKHKSNEYKQM----------LDQ 763
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEelEELIEELE-SELEALLNERASLeealallrseLEE 898
                          250       260       270
                   ....*....|....*....|....*....|
gi 44889014    764 KINGEKILVQQIEDLRRKQIHDEEEKEAMK 793
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLE 928
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
537-793 5.25e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.44  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   537 PIDEKEKLSRLQHsthafeatlivmnrineDNERKLGNISEQYEKKvseLGDLKKMLDEARKKFEEDVEQMKNSNQQvIR 616
Cdd:pfam05622 277 PAEIREKLIRLQH-----------------ENKMLRLGQEGSYRER---LTELQQLLEDANRRKNELETQNRLANQR-IL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   617 NHANAVESLQKTHETQiAEKNKEFERnfeeerarreaevcamnnrhqkvvacLDEKISEAEKQCEQLNVDKKVLQAALAN 696
Cdd:pfam05622 336 ELQQQVEELQKALQEQ-GSKAEDSSL--------------------------LKQKLEEHLEKLHEAQSELQKKKEQIEE 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   697 DCDHRNQMLTKEISSLQTALEMKSAEMK--ELRQKnqnlslqvdeiplkeleisKWKHKSNEYKQMLDQKINGEKI---- 770
Cdd:pfam05622 389 LEPKQDSNLAQKIDELQEALRKKDEDMKamEERYK-------------------KYVEKAKSVIKTLDPKQNPASPpeiq 449
                         250       260
                  ....*....|....*....|....
gi 44889014   771 -LVQQIEDLRRKQIHDEEEKEAMK 793
Cdd:pfam05622 450 aLKNQLLEKDKKIEHLERDFEKSK 473
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
21-85 1.79e-23

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: 94.39  E-value: 1.79e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 44889014    21 IGRLVDVVNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIFAPIFRV 85
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
21-86 3.68e-20

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: 84.94  E-value: 3.68e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 44889014     21 IGRLVDVVNVGK-GFLRYVGPIHGKDGMFCGIELLEPN-GKHDGTFQGVSYFIATPYHGIFAPIFRVT 86
Cdd:smart01052   1 VGDRVEVGGGGRrGTVRYVGPTPFAPGVWVGVELDEPLrGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
28-79 1.70e-05

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: 48.53  E-value: 1.70e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 44889014  28 VNVGKGFLRYVGPIHGKDGMFCGIELLEPNGKHDGTFQGVSYFIATPYHGIF 79
Cdd:COG5244  12 LGDKFGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIF 63
PTZ00121 PTZ00121
MAEBL; Provisional
364-793 9.10e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   364 VKQKAPSKHQlmMEQLKAsiEAEKTKPKKEIKSRVSLLPPPAPKAPQKENKEGGEMTETPRRTITKTPLKTVNAKAKTsp 443
Cdd:PTZ00121 1307 AKKKAEEAKK--ADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA-- 1380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   444 tppvERQKKERKPLYVAPPAKERVEKEKKipsKPVVSPPTTAEKKPVVSSIPSTSSASKGPfptssfaggklQGPRKTSS 523
Cdd:PTZ00121 1381 ----DAAKKKAEEKKKADEAKKKAEEDKK---KADELKKAAAAKKKADEAKKKAEEKKKAD-----------EAKKKAEE 1442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   524 SSTTTSAKKQKNPPIDEKEKLSRLQHSTHAFEATLIVMNRINEDNERKLgniSEQYEKKVSEL---GDLKKMLDEARKKF 600
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK---AEEAKKKADEAkkaAEAKKKADEAKKAE 1519
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   601 E-EDVEQMKNSNQQVIRNHANAVESLQKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKVVACLDEKISEAEKQ 679
Cdd:PTZ00121 1520 EaKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   680 CEQLNVDKKVLQAALANDCDHRNQMLTKEISSLQTALEMKSAEMKELRqKNQNLSLQVDEIPLKELEISKW----KHKSN 755
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAEEENKIKAAEEAKKaeedKKKAE 1678
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 44889014   756 EYKQMLDQKINGEKILVQQIEDLRR-KQIHDEEEKEAMK 793
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKK 1717
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
538-793 2.30e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    538 IDE-KEKLSRLQHSTHAFEATLIVMnrinednERKLGNISEQYEKKVSELGDLKKMLDEARKKFEEDVEQMKNSNQQVIR 616
Cdd:TIGR02168  679 IEElEEKIEELEEKIAELEKALAEL-------RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    617 NHANAVESL-QKTHETQIAEKNKEFERNFEEERARREAEVCAMNNRHQKvvacLDEKISEAEKQCEQLNVDkkvlqaalA 695
Cdd:TIGR02168  752 LSKELTELEaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEE--------A 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014    696 NDCDHRNQMLTKEISSLQTALEMKSAEMKELRQKNQNLSLQVD--EIPLKELEiSKWKHKSNEYKQM----------LDQ 763
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEelEELIEELE-SELEALLNERASLeealallrseLEE 898
                          250       260       270
                   ....*....|....*....|....*....|
gi 44889014    764 KINGEKILVQQIEDLRRKQIHDEEEKEAMK 793
Cdd:TIGR02168  899 LSEELRELESKRSELRRELEELREKLAQLE 928
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
531-781 4.51e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   531 KKQKNPPIDEKEKLSRLQHSTHAFEATLIVMNRINEDNERKLGNISEQYEKKVSELGDLKKMLDEARKKFEEDVEQMKNS 610
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   611 NQQV---------IRNHANAVESLQKTHETQIAEKNKEFERNFEEERarreaevcamNNRHQKVVACLDEKISEAEKQCE 681
Cdd:TIGR04523 509 EEKVkdltkkissLKEKIEKLESEKKEKESKISDLEDELNKDDFELK----------KENLEKEIDEKNKEIEELKQTQK 578
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   682 QLNVDKKVLQAALANDCDHRNQmLTKEISSLQTALEMKSAEMKELRQKNQNLSLQVDEIPLK-----------ELEISKW 750
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKD-LIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKknklkqevkqiKETIKEI 657
                         250       260       270
                  ....*....|....*....|....*....|.
gi 44889014   751 KHKSNEykqmLDQKINGEKILVQQIEDLRRK 781
Cdd:TIGR04523 658 RNKWPE----IIKKIKESKTKIDDIIELMKD 684
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
537-793 5.25e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.44  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   537 PIDEKEKLSRLQHsthafeatlivmnrineDNERKLGNISEQYEKKvseLGDLKKMLDEARKKFEEDVEQMKNSNQQvIR 616
Cdd:pfam05622 277 PAEIREKLIRLQH-----------------ENKMLRLGQEGSYRER---LTELQQLLEDANRRKNELETQNRLANQR-IL 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   617 NHANAVESLQKTHETQiAEKNKEFERnfeeerarreaevcamnnrhqkvvacLDEKISEAEKQCEQLNVDKKVLQAALAN 696
Cdd:pfam05622 336 ELQQQVEELQKALQEQ-GSKAEDSSL--------------------------LKQKLEEHLEKLHEAQSELQKKKEQIEE 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 44889014   697 DCDHRNQMLTKEISSLQTALEMKSAEMK--ELRQKnqnlslqvdeiplkeleisKWKHKSNEYKQMLDQKINGEKI---- 770
Cdd:pfam05622 389 LEPKQDSNLAQKIDELQEALRKKDEDMKamEERYK-------------------KYVEKAKSVIKTLDPKQNPASPpeiq 449
                         250       260
                  ....*....|....*....|....
gi 44889014   771 -LVQQIEDLRRKQIHDEEEKEAMK 793
Cdd:pfam05622 450 aLKNQLLEKDKKIEHLERDFEKSK 473
 
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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